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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Detalles Bibliográficos
Autores principales: Gorbalenya, Alexander E., Koonin, Eugene V., Donchenko, Alexei P., Blinov, Vladimir M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 1988
Materias:
Discussion Letters
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130140/
https://www.ncbi.nlm.nih.gov/pubmed/2841153
http://dx.doi.org/10.1016/0014-5793(88)81226-2
Descripción
Sumario: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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