The microcin J25 β-hairpin region is important for antibiotic uptake but not for RNA polymerase and respiration inhibition

被引：26

作者：

Bellomio, A ^{[1
]}

Vincent, PA ^{[1
]}

de Arcuri, BF ^{[1
]}

Salomón, RA ^{[1
]}

Morero, RD ^{[1
]}

Farías, RN ^{[1
]}

机构：

[1] Univ Nacl Tucuman, Consejo Nacl Invest Cient & Tecn, Inst Super Invest Biol, Dept Bioquim Nutr, RA-4000 San Miguel De Tucuman, Argentina

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 325卷 / 04期

关键词：

microcin J25; FhuA; RNA polymerase; oxygen consumption; thermolysin; SbmA;

D O I：

10.1016/j.bbrc.2004.10.186

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：

The antibiotic microcin J25 (MccJ25) was cleaved by hydrolysis with thermolysin giving a two-chain peptide (MccJ25-Th19) of 10 and 9 amino acid residues. MccJ25-Th19 with deep modifications in P-hairpin region had no effect on Escherichia coli growth, but still inhibited RNA polymerase in vitro and oxygen consumption in Salmonella strains. MccJ25-ThN showed antibiotic activity on E coli transformed with plasmids containing either fhuA or sbmA genes, which code for proteins involved in MccJ25 transport. These results suggest that an intact beta-hairpin region is crucial for MccJ25 import but not for inhibition of E. coli RNA polymerase or oxygen consumption in Salmonella strains. (C) 2004 Elsevier Inc. All rights reserved.

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收藏

页码：1454 / 1458

页数：5

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