Key Points
- Determine the sequence of Xenopus laevis hnRNP K to identify conserved structural domains involved in nucleic acid binding.
- Cloned and sequenced the cDNA of Xenopus laevis hnRNP K.
- Performed comparative sequence homology analysis against human hnRNP K and known nucleic acid-binding proteins across diverse species.
- Xenopus laevis hnRNP K is a 47 kD protein highly similar to human 66 kD hnRNP K, differing primarily by two large internal deletions.
- Identified a 45-amino-acid repeated motif, designated the KH (K homology) motif, that is almost entirely conserved between human and X. laevis proteins.
- Demonstrated significant sequence homology between the KH motif and other RNA-associated proteins, including archaebacterial ribosomal protein S3 and yeast MER1.
Structured PICO
PPopulationXenopus laevis hnRNP K cDNA/protein
IInterventionCloning and sequence analysis
CComparatorHuman hnRNP K protein and other nucleic acid binding proteins
OOutcomeIdentification and sequence homology of the KH motif
Identifies the KH motif in the hnRNP K protein, suggesting its role as a conserved RNA-binding domain.