RECOGNITION OF 2'-HYDROXYL GROUPS BY ESCHERICHIA-COLI RIBONUCLEASE HI

被引：18

作者：

IWAI, S

KATAOKA, S

WAKASA, M

OHTSUKA, E

NAKAMURA, H

机构：

[1] HOKKAIDO UNIV,FAC PHARMACEUT SCI,KITA KU,SAPPORO,HOKKAIDO 060,JAPAN

[2] PROT ENGN RES INST,SUITA,OSAKA 565,JAPAN

来源：

FEBS LETTERS | 1995年 / 368卷 / 02期

关键词：

RIBONUCLEASE H; OLIGONUCLEOTIDE; INTERACTION; HYDROGEN BOND; TERTIARY STRUCTURE;

D O I：

10.1016/0014-5793(95)00683-Z

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：

In order to investigate the hydrogen-bonding interactions between Escherichia coli ribonuclease HI and the 2'-hydroxyl functions of the substrate, oligonucleotide duplexes containing 2'-amino-2'-deoxyuridine or 2'-fluoro-2'-deoxyuridine at a specific site were used, and their affinities for the enzyme were determined by kinetic analyses. The results indicate that the hydroxyl groups of the nucleoside 3'-adjacent to the cleaved phosphodiester linkage and the second nucleoside 5' to the cleaved phosphodiester act as both a proton donor and an acceptor and as a proton acceptor, respectively, in the enzyme-substrate complex. A molecular model was constructed using the interactions derived from the results.

引用

页码：315 / 320

页数：6

共 40 条

[1] SITE-SPECIFIC EXCISION FROM RNA BY RNASE-H AND MIXED-PHOSPHATE-BACKBONE OLIGODEOXYNUCLEOTIDES [J].