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截短的核酸酶肽对粘质沙雷氏菌核酸酶分泌的抑制作用。

Inhibition of Serratia marcescens nuclease secretion by a truncated nuclease peptide.

作者信息

Chen Y C, Suh Y, Riise E, Kartman B, Jin S, Benedik M J

机构信息

Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934, USA.

出版信息

Gene. 1996 Jun 12;172(1):9-16. doi: 10.1016/0378-1119(96)00187-4.

Abstract

The production of extracellular nuclease (Nuc) from the Serratia marcescens nucA chromosomal locus is inhibited in cells producing the N-terminal portion of Nuc from a multicopy plasmid. This inhibition in trans is not at the level of nucA expression, but rather at the level of secretion of the Nuc protein. Production of the periplasmic protein beta-lactamase (Bla) does not inhibit Nuc production unless fused to the nucA signal peptide and expressed from nucAp. Inhibition by either the truncated Nuc peptide (delta Nuc) or a Bla fusion protein is promoter specific and observed when expressed from nucAp; little inhibition is observed when the same protein is expressed from the lacZpo promoter-operator. This promoter specificity is also true for the secretion of Nuc itself.

摘要

粘质沙雷氏菌nucA染色体位点产生的细胞外核酸酶(Nuc)在从多拷贝质粒产生Nuc N端部分的细胞中受到抑制。这种反式抑制不是在nucA表达水平,而是在Nuc蛋白的分泌水平。周质蛋白β-内酰胺酶(Bla)的产生不会抑制Nuc的产生,除非与nucA信号肽融合并从nucAp表达。截短的Nuc肽(δNuc)或Bla融合蛋白的抑制作用具有启动子特异性,当从nucAp表达时可观察到;当从lacZpo启动子-操纵子表达相同蛋白时,几乎观察不到抑制作用。这种启动子特异性对于Nuc本身的分泌也是如此。

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