ENDONUCLEASE (R)-SUBUNITS OF TYPE-I AND TYPE-III RESTRICTION-MODIFICATION ENZYMES CONTAIN A HELICASE-LIKE DOMAIN

被引：96

作者：

GORBALENYA, AE ^{[1
]}

KOONIN, EV ^{[1
]}

机构：

[1] ACAD SCI USSR, INST MICROBIOL, MOSCOW 117811, USSR

来源：

FEBS LETTERS | 1991年 / 291卷 / 02期

关键词：

AMINO ACID COMPARISON; SEQUENCE PATTERN; ATP-BINDING SITE; HELICASE; RESTRICTASE;

D O I：

10.1016/0014-5793(91)81301-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A statistically significant amino acid sequence similarity is demonstrated between the endonuclease (R) subunit of EcoK restriction-modification (R-M) enzyme, and RNA and DNA helicases of the so-called 'DEAD' family. It is further shown that all three known sequences of R subunits of type-I and type-III R-M enzymes contain the conserved amino acid sequence motifs typical of the previously described helicase superfamily II [(1989) Nucleic Acids Res. 17, 4713-4730]. A hypothesis is proposed that these enzymes may exert helicase activity possibly required for local unwinding of DNA in the cleavage sites.

引用

页码：277 / 281

页数：5

共 19 条

[1] RADH, A GENE OF SACCHAROMYCES-CEREVISIAE ENCODING A PUTATIVE DNA HELICASE INVOLVED IN DNA-REPAIR - CHARACTERISTICS OF RADH MUTANTS AND SEQUENCE OF THE GENE [J].