The bacteriophage T4 GroES homologue, gp31, in conjunction with the Escherichia coli chaperonin GroEL, is both necessary and sufficient to fold the T4 major capsid protein, gp23, to a state competent for capsid assembly as shown by in vivo expression studies. GroES is unable to function in this role as a productive co-chaperonin. The sequencing and characterization of mutations within gp23 that confer GroEL and gp31 chaperonin-independent folding of the mutant protein suggest that the chaperonin requirements are due to specific sequence determinants or structures in critical regions of gp23 that behave in an additive fashion to confer a chaperonin bypass phenotype. Conservative amino acid substitutions in these critical regions enable gp23 to fold in a GroEL-gp31 chaperonin-independent mode, albeit less efficiently than wild type, both in vivo and in vitro. Although the presence of functional GroEL-gp31 enhances folding of the mutated gp23in vivo, GroEL-GroES has no such effect. Site-directed mutagenesis experiments suggest that a translational pausing mechanism is not responsible for the bypass mutant phenotype. Polyhead reassembly experiments are also consistent with direct, post-translational effects of the bypass mutations on polypeptide folding. Given our finding that gp31 is not required for the binding of the major capsid protein to GroEL and that active GroES is incapable of folding the gp23 polypeptide chain to native conformation, our results suggest co-chaperonin specificity in the folding of certain substrates. The bacteriophage T4 GroES homologue, gp31, in conjunction with the Escherichia coli chaperonin GroEL, is both necessary and sufficient to fold the T4 major capsid protein, gp23, to a state competent for capsid assembly as shown by in vivo expression studies. GroES is unable to function in this role as a productive co-chaperonin. The sequencing and characterization of mutations within gp23 that confer GroEL and gp31 chaperonin-independent folding of the mutant protein suggest that the chaperonin requirements are due to specific sequence determinants or structures in critical regions of gp23 that behave in an additive fashion to confer a chaperonin bypass phenotype. Conservative amino acid substitutions in these critical regions enable gp23 to fold in a GroEL-gp31 chaperonin-independent mode, albeit less efficiently than wild type, both in vivo and in vitro. Although the presence of functional GroEL-gp31 enhances folding of the mutated gp23in vivo, GroEL-GroES has no such effect. Site-directed mutagenesis experiments suggest that a translational pausing mechanism is not responsible for the bypass mutant phenotype. Polyhead reassembly experiments are also consistent with direct, post-translational effects of the bypass mutations on polypeptide folding. Given our finding that gp31 is not required for the binding of the major capsid protein to GroEL and that active GroES is incapable of folding the gp23 polypeptide chain to native conformation, our results suggest co-chaperonin specificity in the folding of certain substrates. polymerase chain reaction isopropyl-1-thio-β-d-galactopyranoside wild type multiplicity of infection polyacrylamide gel electrophoresis N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine. GroEL and its co-chaperonin, GroES, are stress-inducible proteins, synthesized from the groE operon of Escherichia coli (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google Scholar, 2Tilly K. Murialdo H. Georgopoulos C. Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 1629-1633Crossref PubMed Scopus (108) Google Scholar). GroEL and GroES are members of the chaperonin or Cpn60/Cpn10 family of proteins and are thought to be general catalysts unrestricted in ability to fold proteins by interacting reversibly with polypeptides to passively prevent or deter incorrect protein folding and aggregation (3Hendrick J.P. Hartl F.U. Annu. Rev. Biochem. 1993; 62: 349-384Crossref PubMed Scopus (1461) Google Scholar, 4Zeilstra-Ryalls J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). The mechanism of chaperonin-mediated polypeptide folding involves the of GroEL with GroES and of the native GroEL and GroES are required for coli and GroEL has shown to to of coli proteins in that the the ability to with a of polypeptide O. Georgopoulos C. J. Bacteriol. PubMed Scopus Google Scholar, A. Sci. PubMed Scopus Google is synthesized as a a with K. Proc. Natl. Acad. Sci. U. S. A. 1993; PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). The GroEL has the with an of enable to a protein in the to GroES binding K. A. PubMed Scopus Google Scholar). The GroEL co-chaperonin, GroES, a of K. C. Georgopoulos C. J. PubMed Google Scholar, H. S. A. 1991; PubMed Scopus Google Scholar, S. PubMed Scopus Google Scholar, J. PubMed Scopus Google Scholar). of the GroEL the of the in the GroEL an in polypeptide K. PubMed Scopus Google and major with the of and GroES that the of the GroEL folding to the folding of proteins in S. PubMed Scopus Google H. PubMed Scopus Google Scholar). experiments suggest a critical role for GroES as an in the binding and of the polypeptide in experiments folding of proteins in the of the co-chaperonin K. J. Scholar, J. 1993; PubMed Scopus Google Scholar, C. J. PubMed Scopus Google in of the co-chaperonin for folding a be as with in vivo the of the co-chaperonin in protein folding to be to role in the folding of GroEL and GroES are in assembly (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google A. Georgopoulos C. PubMed Scopus Google A. J. Bacteriol. PubMed Google J. PubMed Scopus Google and PubMed Scopus Google both GroEL and GroES for bacteriophage T4 is not by of the mutations in the the coli GroES co-chaperonin. bacteriophage T4 infection the major capsid protein is synthesized as that a shown to be of of that bacteriophage T4 a bacteriophage protein that is required to its major capsid protein, gp23, this be of the major capsid protein in vivo the of J. PubMed Scopus Google Scholar). as gp31, with the coli protein, GroEL, in the folding of gp23 J. Scholar, A. A. H. J. PubMed Scopus Google Scholar, C. PubMed Scopus Google Scholar, H. J. PubMed Google Scholar, PubMed Scopus Google Scholar). of the of GroEL, gp31, and the T4 major capsid protein is by mutations in the the major capsid protein that to the gp31 J. PubMed Google Scholar). mutations in T4 the in the no structures are and the of gp23 is to certain mutations in are to mutations that T4 capsid assembly in an T4 gp31 to GroES as the co-chaperonin for GroEL PubMed Scopus Google Scholar, Georgopoulos C. PubMed Scopus Google of the chaperonin and protein to be The this is both and J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). The of the coli chaperonin by bacteriophage T4 an to the role of the co-chaperonin in chaperonin-mediated protein folding. the specificity for T4 gp31 in conjunction with GroEL to fold gp23 has not in T4 infection and and these proteins with of and coli are or for of for of specificity are also synthesized Scholar). to by in vivo expression the for the T4 gp31 as this is a of to the due to protein folding requirements assembly or is specificity in the folding of the T4 major capsid protein that a that the coli is of protein this expression to that of with in the presence of GroEL, is necessary and sufficient to structures in vivo and that GroES is unable to function in this are of gp23, folding and of the major capsid protein and are thought to the in active T4 of for is of Although folding and of the major capsid protein GroEL and gp31, that are in the of both proteins by T4 of mutations in the major capsid protein, vivo and in vitro. and of mutant are to in the of mutations that confer chaperonin-independent folding to the mutant gp23 protein in an additive suggest that the ability of the protein to fold of chaperonin is to certain sequence determinants within the major capsid of of these to the specificity of amino acid that confer the its chaperonin and a mechanism of translational pausing J. PubMed Scopus Google Scholar, Sci. PubMed Scopus Google protein folding in the of that a bacteriophage T4 GroES is required to fold the major capsid protein of specific in the gp23 these mutations in the gp23 polypeptide confer chaperonin-independent folding. of the bypass mutations is by the of a of coli that the are to of specific GroEL, gp31, and GroES mutations and these the of its function in the folding be in the that of the GroEL and GroES are by the T4 the that the mutations the major capsid protein as to productive with specific functional or that gp23 be mutated as to be in folding by The that the to in the presence of gp31 and GroEL not than in also that the mutant polypeptide are not to a chaperonin folding to be on by the the GroEL and in the folding of the protein is also by in experiments of gp23 chaperonin-independent folding of the mutant chaperonin family is for of and J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). Although the GroES and gp31 both with GroEL, is no sequence the the or PubMed Scopus Google Scholar, Georgopoulos C. PubMed Scopus Google Scholar). to be in the in the of both proteins A. Georgopoulos C. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar, J. Fayet O. Georgopoulos C. 1993; PubMed Scopus Google Scholar). to GroES gp31 are K. C. Georgopoulos C. J. PubMed Google Scholar, PubMed Scopus Google and to structures in vivo J. in the of the T4 of Scholar). the that gp31 in a state in gp31 as with J. Scholar, J. A. PubMed Scopus Google Scholar). in of these is not that with GroEL in that assembly in the presence of proteins, is than in less than the that in the of proteins, gp23 than in an PubMed Scopus Google J. PubMed Google be from experiments a general co-chaperonin role of gp31 A. Georgopoulos C. PubMed Scopus Google that gp31 with GroEL fold a of proteins in the the of the mutations that such with T4 than gp23, are of that both GroES and gp31 are in and of the of suggest that the GroEL-gp31 be the members of the bacteriophage family and that is J. in the of the T4 of Scholar). has that is not in members of the family that the sequence is also the suggest gp31 has to the folding of the T4 major capsid protein that are the of the GroEL-GroES and the of an of specificity in chaperonin of this and this not be J. PubMed Google Scholar). mutations as of or to the and that a of such mutant in J. PubMed Google Scholar, J. PubMed Google Scholar). bypass regions sequence to the T4 protein K. J. PubMed Scopus Google has in to the and mutations and and mutations in in these of for Scholar, K. J. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). of these mutant are thought to this be also to be critical for the folding of the major capsid of the GroEL-gp31 chaperonin bypass mutations on the major capsid protein gp23 and polypeptide of for Scholar, PubMed Scopus Google Scholar). The of of and and mutations are The amino acid from and mutations are the polypeptide The on the polypeptide regions of to the capsid protein, the of and chaperonin mutations in the the of from the to to or of such of the gp23 assembly the specificity of the T4 major capsid protein for the gp31 co-chaperonin be in to for protein folding and chaperonin structures K. Proc. Natl. Acad. Sci. U. S. A. 1993; PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, K. A. PubMed Scopus Google Scholar, K. PubMed Scopus Google Scholar, J. Hartl F.U. 1993; PubMed Scopus Google Scholar, F.U. PubMed Scopus Google Scholar). is that has a on GroES T4 to a this are to of from expression effects on not GroES of gp23 to the folding of GroEL, GroEL with the gp31 co-chaperonin our experiments of or with that gp23, with and gp31 be with that gp31 is not required for gp23 or binding to GroEL that is required for the productive folding of the in the binding of gp31 to GroEL a folding than GroES is to GroEL also the The gp31 with GroEL gp23 is within the folding GroES be from by the be consistent with the T4 major capsid protein and its of the gp31 this and this mechanism J. PubMed Scopus Google Scholar). that is an to the The ability of the GroEL-GroES to fold proteins than gp23, such as the bacteriophage protein or protein that the of the folding not the gp31 (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google Scholar, A. J. Bacteriol. PubMed Google Scholar). the that the folding requirements are less by the T4 chaperonin the folding this is the chaperonin specificity results in this to on for GroEL for these specificity results is that GroES the of gp23 from GroEL, gp31 the in folding in the that GroEL by gp31 specific with gp23 that not with the GroEL-GroES and that these enable the polypeptide to native a consistent with the of gp23 folding by gp31 in a T4 this the major capsid protein sequence not of the folding as the mutations folding to the gp23 polypeptide chaperonin-independent gp31 the GroEL chaperonin in such a that specific folding to the gp23 by a is to that the of the bypass amino acid to a chaperonin-independent folding to GroEL chaperonin on these of the polypeptide this the role of the GroEL-gp31 chaperonin not be to the folding from aggregation specific to an that for folding of specific or Although the of the T4 major capsid protein is not has shown to a to the its assembly to is in a state in the of for Scholar, J. 1991; PubMed Scopus Google Scholar). this is to the specific co-chaperonin assembly to be GroEL and its co-chaperonin, GroES, are stress-inducible proteins, synthesized from the groE operon of Escherichia coli (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google Scholar, 2Tilly K. Murialdo H. Georgopoulos C. Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 1629-1633Crossref PubMed Scopus (108) Google Scholar). GroEL and GroES are members of the chaperonin or Cpn60/Cpn10 family of proteins and are thought to be general catalysts unrestricted in ability to fold proteins by interacting reversibly with polypeptides to passively prevent or deter incorrect protein folding and aggregation (3Hendrick J.P. Hartl F.U. Annu. Rev. Biochem. 1993; 62: 349-384Crossref PubMed Scopus (1461) Google Scholar, 4Zeilstra-Ryalls J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). The mechanism of chaperonin-mediated polypeptide folding involves the of GroEL with GroES and of the native GroEL and GroES are required for coli and GroEL has shown to to of coli proteins in that the the ability to with a of polypeptide O. Georgopoulos C. J. Bacteriol. PubMed Scopus Google Scholar, A. Sci. PubMed Scopus Google Scholar). GroEL is synthesized as a a with K. Proc. Natl. Acad. Sci. U. S. A. 1993; PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). The GroEL has the with an of enable to a protein in the to GroES binding K. A. PubMed Scopus Google Scholar). The GroEL co-chaperonin, GroES, a of K. C. Georgopoulos C. J. PubMed Google Scholar, H. S. A. 1991; PubMed Scopus Google Scholar, S. PubMed Scopus Google Scholar, J. PubMed Scopus Google Scholar). of the GroEL the of the in the GroEL an in polypeptide K. PubMed Scopus Google and major with the of and GroES that the of the GroEL folding to the folding of proteins in S. PubMed Scopus Google H. PubMed Scopus Google Scholar). experiments suggest a critical role for GroES as an in the binding and of the polypeptide in experiments folding of proteins in the of the co-chaperonin K. J. Scholar, J. 1993; PubMed Scopus Google Scholar, C. J. PubMed Scopus Google in of the co-chaperonin for folding a be as with in vivo the of the co-chaperonin in protein folding to be to role in the folding of GroEL and GroES are in assembly (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google A. Georgopoulos C. PubMed Scopus Google A. J. Bacteriol. PubMed Google J. PubMed Scopus Google and PubMed Scopus Google both GroEL and GroES for bacteriophage T4 is not by of the mutations in the the coli GroES co-chaperonin. bacteriophage T4 infection the major capsid protein is synthesized as that a shown to be of of that bacteriophage T4 a bacteriophage protein that is required to its major capsid protein, gp23, this be of the major capsid protein in vivo the of J. PubMed Scopus Google Scholar). as gp31, with the coli protein, GroEL, in the folding of gp23 J. Scholar, A. A. H. J. PubMed Scopus Google Scholar, C. PubMed Scopus Google Scholar, H. J. PubMed Google Scholar, PubMed Scopus Google Scholar). of the of GroEL, gp31, and the T4 major capsid protein is by mutations in the the major capsid protein that to the gp31 J. PubMed Google Scholar). mutations in T4 the in the no structures are and the of gp23 is to certain mutations in are to mutations that T4 capsid assembly in an T4 gp31 to GroES as the co-chaperonin for GroEL PubMed Scopus Google Scholar, Georgopoulos C. PubMed Scopus Google Scholar). The of the chaperonin and protein to be The this is both and J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). The of the coli chaperonin by bacteriophage T4 an to the role of the co-chaperonin in chaperonin-mediated protein folding. the specificity for T4 gp31 in conjunction with GroEL to fold gp23 has not in T4 infection and and these proteins with of and coli are or for of for of specificity are also synthesized Scholar). to by in vivo expression the for the T4 gp31 as this is a of to the due to protein folding requirements assembly or is specificity in the folding of the T4 major capsid protein that a that the coli is of protein folding. this expression to that of with in the presence of GroEL, is necessary and sufficient to structures in vivo and that GroES is unable to function in this are of gp23, folding and of the major capsid protein and are thought to the in active T4 of for is of Although folding and of the major capsid protein GroEL and gp31, that are in the of both proteins by T4 of mutations in the major capsid protein, vivo and in vitro. and of mutant are to in the of mutations that confer chaperonin-independent folding to the mutant gp23 protein in an additive suggest that the ability of the protein to fold of chaperonin is to certain sequence determinants within the major capsid of of these to the specificity of amino acid that confer the its chaperonin and a mechanism of translational pausing J. PubMed Scopus Google Scholar, Sci. PubMed Scopus Google protein folding in the of that a bacteriophage T4 GroES is required to fold the major capsid protein of specific in the gp23 these mutations in the gp23 polypeptide confer chaperonin-independent folding. of the bypass mutations is by the of a of coli that the are to of specific GroEL, gp31, and GroES mutations and these the of its function in the folding be in the that of the GroEL and GroES are by the T4 the that the mutations the major capsid protein as to productive with specific functional or that gp23 be mutated as to be in folding by The that the to in the presence of gp31 and GroEL not than in also that the mutant polypeptide are not to a chaperonin folding to be on by the the GroEL and in the folding of the protein is also by in experiments of gp23 chaperonin-independent folding of the mutant chaperonin family is for of and J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). Although the GroES and gp31 both with GroEL, is no sequence the the or PubMed Scopus Google Scholar, Georgopoulos C. PubMed Scopus Google Scholar). to be in the in the of both proteins A. Georgopoulos C. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar, J. Fayet O. Georgopoulos C. 1993; PubMed Scopus Google Scholar). to GroES gp31 are K. C. Georgopoulos C. J. PubMed Google Scholar, PubMed Scopus Google and to structures in vivo J. in the of the T4 of Scholar). the that gp31 in a state in gp31 as with J. Scholar, J. A. PubMed Scopus Google Scholar). in of these is not that with GroEL in that assembly in the presence of proteins, is than in less than the that in the of proteins, gp23 than in an PubMed Scopus Google J. PubMed Google be from experiments a general co-chaperonin role of gp31 A. Georgopoulos C. PubMed Scopus Google that gp31 with GroEL fold a of proteins in the the of the mutations that such with T4 than gp23, are of that both GroES and gp31 are in and of the of suggest that the GroEL-gp31 be the members of the bacteriophage family and that is J. in the of the T4 of Scholar). has that is not in members of the family that the sequence is also the suggest gp31 has to the folding of the T4 major capsid protein that are the of the GroEL-GroES and the of an of specificity in chaperonin of this and this not be J. PubMed Google Scholar). mutations as of or to the and that a of such mutant in J. PubMed Google Scholar, J. PubMed Google Scholar). bypass regions sequence to the T4 protein K. J. PubMed Scopus Google has in to the and mutations and and mutations in in these of for Scholar, K. J. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). of these mutant are thought to this be also to be critical for the folding of the major capsid specificity of the T4 major capsid protein for the gp31 co-chaperonin be in to for protein folding and chaperonin structures K. Proc. Natl. Acad. Sci. U. S. A. 1993; PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, K. A. PubMed Scopus Google Scholar, K. PubMed Scopus Google Scholar, J. Hartl F.U. 1993; PubMed Scopus Google Scholar, F.U. PubMed Scopus Google Scholar). is that has a on GroES T4 to a this are to of from expression effects on not GroES of gp23 to the folding of GroEL, GroEL with the gp31 co-chaperonin our experiments of or with that gp23, with and gp31 be with that gp31 is not required for gp23 or binding to GroEL that is required for the productive folding of the in the binding of gp31 to GroEL a folding than GroES is to GroEL also the The gp31 with GroEL gp23 is within the folding GroES be from by the be consistent with the T4 major capsid protein and its of the gp31 this and this mechanism J. PubMed Scopus Google Scholar). that is an to the The ability of the GroEL-GroES to fold proteins than gp23, such as the bacteriophage protein or protein that the of the folding not the gp31 (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google Scholar, A. J. Bacteriol. PubMed Google Scholar). the that the folding requirements are less by the T4 chaperonin the folding this is the chaperonin specificity results in this to on for GroEL for these specificity results is that GroES the of gp23 from GroEL, gp31 the in folding in the that GroEL by gp31 specific with gp23 that not with the GroEL-GroES and that these enable the polypeptide to native a consistent with the of gp23 folding by gp31 in a T4 this the major capsid protein sequence not of the folding as the mutations folding to the gp23 polypeptide chaperonin-independent gp31 the GroEL chaperonin in such a that specific folding to the gp23 by a is to that the of the bypass amino acid to a chaperonin-independent folding to GroEL chaperonin on these of the polypeptide this the role of the GroEL-gp31 chaperonin not be to the folding from aggregation specific to an that for folding of specific or Although the of the T4 major capsid protein is not has shown to a to the its assembly to is in a state in the of for Scholar, J. 1991; PubMed Scopus Google Scholar). this is to the specific co-chaperonin assembly to be that a bacteriophage T4 GroES is required to fold the major capsid protein of specific in the gp23 these mutations in the gp23 polypeptide confer chaperonin-independent folding. of the bypass mutations is by the of a of coli that the are to of specific GroEL, gp31, and GroES mutations and these the of its function in the folding be in the that of the GroEL and GroES are by the T4 the that the mutations the major capsid protein as to productive with specific functional or that gp23 be mutated as to be in folding by The that the to in the presence of gp31 and GroEL not than in also that the mutant polypeptide are not to a chaperonin folding to be on by the the GroEL and in the folding of the protein is also by in experiments of gp23 chaperonin-independent folding of the mutant The chaperonin family is for of and J. Fayet O. Georgopoulos C. Annu. Rev. Microbiol. 1991; 45: 301-325Crossref PubMed Scopus (221) Google Scholar). Although the GroES and gp31 both with GroEL, is no sequence the the or PubMed Scopus Google Scholar, Georgopoulos C. PubMed Scopus Google Scholar). to be in the in the of both proteins A. Georgopoulos C. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar, J. Fayet O. Georgopoulos C. 1993; PubMed Scopus Google Scholar). to GroES gp31 are K. C. Georgopoulos C. J. PubMed Google Scholar, PubMed Scopus Google and to structures in vivo J. in the of the T4 of Scholar). the that gp31 in a state in gp31 as with J. Scholar, J. A. PubMed Scopus Google Scholar). in of these is not that with GroEL in that assembly in the presence of proteins, is than in less than the that in the of proteins, gp23 than in an PubMed Scopus Google J. PubMed Google Scholar). Although be from experiments a general co-chaperonin role of gp31 A. Georgopoulos C. PubMed Scopus Google that gp31 with GroEL fold a of proteins in the the of the mutations that such with T4 than gp23, are of that both GroES and gp31 are in and of the of suggest that the GroEL-gp31 be the members of the bacteriophage family and that is J. in the of the T4 of Scholar). has that is not in members of the family that the sequence is also the suggest gp31 has to the folding of the T4 major capsid protein that are the of the GroEL-GroES and the of an of specificity in chaperonin The of this and this not be J. PubMed Google Scholar). mutations as of or to the and that a of such mutant in J. PubMed Google Scholar, J. PubMed Google Scholar). bypass regions sequence to the T4 protein K. J. PubMed Scopus Google has in to the and mutations and and mutations in in these of for Scholar, K. J. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). of these mutant are thought to this be also to be critical for the folding of the major capsid The specificity of the T4 major capsid protein for the gp31 co-chaperonin be in to for protein folding and chaperonin structures K. Proc. Natl. Acad. Sci. U. S. A. 1993; PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, K. A. PubMed Scopus Google Scholar, K. PubMed Scopus Google Scholar, J. Hartl F.U. 1993; PubMed Scopus Google Scholar, F.U. PubMed Scopus Google Scholar). is that has a on GroES T4 to a this are to of from expression effects on not GroES of gp23 to the folding of GroEL, GroEL with the gp31 co-chaperonin our experiments of or with that gp23, with and gp31 be with that gp31 is not required for gp23 or binding to GroEL that is required for the productive folding of the in the binding of gp31 to GroEL a folding than GroES is to GroEL also the The gp31 with GroEL gp23 is within the folding GroES be from by the be consistent with the T4 major capsid protein and its of the gp31 this and this mechanism J. PubMed Scopus Google Scholar). that is an to the The ability of the GroEL-GroES to fold proteins than gp23, such as the bacteriophage protein or protein that the of the folding not the gp31 (1Tilly K. Georgopoulos C. J. Bacteriol. 1982; 149: 1082-1088Crossref PubMed Google Scholar, A. J. Bacteriol. PubMed Google Scholar). the that the folding requirements are less by the T4 chaperonin the folding this is the chaperonin specificity results in this to on for GroEL folding. for these specificity results is that GroES the of gp23 from GroEL, gp31 the in folding in the that GroEL by gp31 specific with gp23 that not with the GroEL-GroES and that these enable the polypeptide to native a consistent with the of gp23 folding by gp31 in a T4 this the major capsid protein sequence not of the folding as the mutations folding to the gp23 polypeptide chaperonin-independent gp31 the GroEL chaperonin in such a that specific folding to the gp23 by a is to that the of the bypass amino acid to a chaperonin-independent folding to GroEL chaperonin on these of the polypeptide this the role of the GroEL-gp31 chaperonin not be to the folding from aggregation specific to an that for folding of specific or Although the of the T4 major capsid protein is not has shown to a to the its assembly to is in a state in the of for Scholar, J. 1991; PubMed Scopus Google Scholar). this is to the specific co-chaperonin assembly to be H. for with for with of gp31 and for with the sequencing of the also for the for the GroES Georgopoulos for the for and for with to and and for on the
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