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

FEBS Letters

Gorbalenya, Alexander E.¹  Koonin, Eugene V.¹  Blinov, Vladimir M.¹  Donchenko, Alexei P.¹ 

[1] Institute of Poliomyelitis and Viral Encephalitides of the USSR Academy of Medical Sciences, 142782 Moscow Region, USSR

关键词: ATP binding;    Eukaryotic virus;    Helicase;    Amino acid sequence;    Sequence comparison;    Nucleoside triphosphate-binding motif;    Protein evolution;    CMV;    cucumber mosaic virus (tricornavirus);    BMV;    brome mosaic virus (tricornavirus);    AlMV;    alfalfa mosaic virus (tricornavirus);    TMV;    tobacco mosaic virus (tobamovirus);    TRV;    tobacco rattle virus (tobravirus);    BSMV;    barley stripe mosaic virus (hordeivirus);    SNBV;    Sindbis virus (alphavirus);    SFV;    Semliki forest virus (alphavirus);    BNYVV;    beet necrotic yellow vein virus (furovirus);    PVX;    potato virus X (polexvirus);    WClMV;    white clover mosaic virus (potex-virus);    IBV;    avian infectious bronchitis virus (coronavirus);    VZV;    varicella zoster virus (herpesvirus);    EBV;    Epstein-Barr virus (herpesvirus);   

DOI  :  10.1016/0014-5793(88)81226-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown