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

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....

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Veröffentlicht in:FEBS letters 1988-08, Vol.235 (1), p.16-24
Hauptverfasser: Gorbalenya, Alexander E., Koonin, Eugene V., Donchenko, Alexei P., Blinov, Vladimir M.
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Sprache:eng
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Zusammenfassung: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)81226-2