A highly active S1-P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c-di-GMP

被引：1

作者：

Hustakova, Blanka ^{[1
,2
,3
]}

Trundova, Maria ^{[1
]}

Adamkova, Kristyna ^{[1
,2
]}

Koval, Tomas ^{[1
]}

Duskova, Jarmila ^{[1
]}

Dohnalek, Jan ^{[1
,3
]}

机构：

[1] Czech Acad Sci, Inst Biotechnol, Biocev, Lab Struct & Funct Biomol, Vestec, Czech Republic

[2] Univ Chem & Technol, Dept Biochem & Microbiol, Prague, Czech Republic

[3] Czech Acad Sci, Inst Biotechnol, Biocev, Prumyslova 595, Vestec 25250, Czech Republic

来源：

FEBS LETTERS | 2023年 / 597卷 / 16期

关键词：

c-di-GMP; cyclic diguanylate; nosocomial infection; S1-P1; nuclease; Stenotrophomonas maltophilia; N-GLYCOSYLATION; PHOSPHODIESTERASE; MECHANISM; ENZYME; TBN1;

D O I：

10.1002/1873-3468.14683

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 number of multidrug-resistant bacterial pathogens code for S1-P1 nucleases with a poorly understood role. We have characterized a recombinant form of S1-P1 nuclease from Stenotrophomonas maltophilia, an opportunistic pathogen. S. maltophilia nuclease 1 (SmNuc1) acts predominantly as an RNase and is active in a wide range of temperatures and pH. It retains a notable level of activity towards RNA and ssDNA at pH 5 and 9 and about 10% of activity towards RNA at 10 degrees C. SmNuc1 with very high catalytic rates out-performs S1 nuclease from Aspergillus oryzae and other similar nucleases on all types of substrates. SmNuc1 degrades second messenger c-di-GMP, which has potential implications for its role in the pathogenicity of S. maltophilia.

引用

页码：2103 / 2118

页数：16

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