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
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页码:277 / 281
页数:5
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