A novel superfamily of nucleoside triphosphate‐binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination

Alexander E. Gorbalenya; Eugene V. Koonin; Alexei P. Donchenko; Vladimir M. Blinov

doi:10.1016/0014-5793(88)81226-2

August 1, 1988FEBS LettersOpen Access

A novel superfamily of nucleoside triphosphate‐binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination

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Key Points

To determine whether sequence similarities exist among NTP-binding proteins in bacteria and viruses, establishing whether they form a shared helicase superfamily involved in nucleic acid unwinding.
Conducted amino acid sequence alignment and statistical similarity analyses across four Escherichia coli helicases or helicase subunits, non-structural proteins of positive-strand RNA viruses, and two herpesvirus proteins.
Applied secondary structure prediction techniques to construct a generalized structural model for the conserved ATP-binding core.
Detected statistically significant sequence similarity within NTP-binding motifs shared across bacterial helicases, eukaryotic positive-strand RNA viruses, and herpesviruses.
Formulated a generalized structural model of the ATP-binding core, defining a unified superfamily of helicases that drive NTP-dependent duplex unwinding during DNA and RNA replication and recombination.

Structured PICO

P

Population

Amino acid sequences of 4 Escherichia coli helicases and helicase subunits, a family of non-structural proteins of eukaryotic positive-strand RNA viruses, and 2 herpesvirus proteins

I

Intervention

Sequence analysis and secondary structure predictions

O

Outcome

Identification of sequence similarity and structural model for the ATP-binding core

Identifies a novel superfamily of helicases involved in NTP-dependent duplex unwinding during DNA and RNA replication and recombination based on sequence similarity.

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Implication

Proposes a new helicase superfamily via sequence similarity; hypothesis-generating for NTP-dependent unwinding pending experimental validation.

Abstract

A statistically significant similarity was demonstrated between the amino acid sequences of 4 Escherichia coli helicases and helicase subunits, a family of non-structural proteins of eukaryotic positive-strand RNA viruses and 2 herpesvirus proteins all of which contain an NTP-binding sequence motif. Based on sequence analysis and secondary structure predictions, a generalized structural model for the ATP-binding core is proposed. It is suggested that all these proteins constitute a superfamily of helicases (or helicase subunits) involved in NTP-dependent duplex unwinding during DNA and RNA replication and recombination.

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Cite This Study

Gorbalenya et al. (1988) studied this question.

synapsesocial.com/papers/6a7050f278a11c550e0a2e7a https://doi.org/10.1016/0014-5793(88)81226-2

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A novel superfamily of nucleoside triphosphate‐binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination

Key Points

Structured PICO

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

A novel superfamily of nucleoside triphosphate‐binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination

Key Points

Structured PICO

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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