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
收藏
页码：2103 / 2118
页数：16
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