SipY是天蓝色链霉菌I型信号肽酶，对蛋白质分泌有重大影响。
SipY Is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion.
作者信息
Palacín Arantxa, Parro Víctor, Geukens Nick, Anné Jozef, Mellado Rafael P
机构信息
Centro Nacional de Biotecnología, Campus de la Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain.
出版信息
J Bacteriol. 2002 Sep;184(17):4875-80. doi: 10.1128/JB.184.17.4875-4880.2002.
Abstract
Most bacteria contain one type I signal peptidase (SPase) for cleavage of signal peptides from secreted proteins. The developmental complex bacterium Streptomyces lividans has the ability to produce and secrete a significant amount of proteins and has four different type I signal peptidases genes (sipW, sipX, sipY, and sipZ) unusually clustered in its chromosome. Functional analysis of the four SPases was carried out by phenotypical and molecular characterization of the different individual sip mutants. None of the sip genes seemed to be essential for bacterial growth. Analysis of total extracellular proteins indicated that SipY is likely to be the major S. lividans SPase, since the sipY mutant strain is highly deficient in overall protein secretion and extracellular protease production, showing a delayed sporulation phenotype when cultured in solid medium.
摘要
大多数细菌含有一种I型信号肽酶（SPase），用于从分泌蛋白中切割信号肽。发育复杂的细菌淡紫链霉菌有能力产生和分泌大量蛋白质，并且在其染色体上有四个不同的I型信号肽酶基因（sipW、sipX、sipY和sipZ）异常聚集。通过对不同单个sip突变体进行表型和分子特征分析，对这四种SPase进行了功能分析。似乎没有一个sip基因对细菌生长是必需的。对总细胞外蛋白的分析表明，SipY可能是淡紫链霉菌的主要SPase，因为sipY突变体菌株在总体蛋白分泌和细胞外蛋白酶产生方面高度缺陷，在固体培养基中培养时表现出延迟的孢子形成表型。
相似文献
1
SipY Is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion.
J Bacteriol. 2002 Sep;184(17):4875-80. doi: 10.1128/JB.184.17.4875-4880.2002.
2
Membrane topology of the Streptomyces lividans type I signal peptidases.
J Bacteriol. 2001 Aug;183(16):4752-60. doi: 10.1128/JB.183.16.4752-4760.2001.
3
Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis.
Proteomics. 2006 Jul;6(14):4137-46. doi: 10.1002/pmic.200500927.
4
Functional analysis of the Streptomyces lividans type I signal peptidases.
Arch Microbiol. 2001 Nov;176(5):377-80. doi: 10.1007/s002030100335.
5
Physical requirements for in vitro processing of the Streptomyces lividans signal peptidases.
J Biotechnol. 2002 Jun 13;96(1):79-91. doi: 10.1016/s0168-1656(02)00039-1.
6
Surface plasmon resonance-based interaction studies reveal competition of Streptomyces lividans type I signal peptidases for binding preproteins.
Microbiology (Reading). 2006 May;152(Pt 5):1441-1450. doi: 10.1099/mic.0.28734-0.
7
Contribution of the multiple Type I signal peptidases to the secretome of Listeria monocytogenes: deciphering their specificity for secreted exoproteins by exoproteomic analysis.
J Proteomics. 2015 Mar 18;117:95-105. doi: 10.1016/j.jprot.2015.01.007. Epub 2015 Jan 28.
8
Differential roles of multiple signal peptidases in the virulence of Listeria monocytogenes.
Mol Microbiol. 2004 Mar;51(5):1251-66. doi: 10.1111/j.1365-2958.2004.03916.x.
9
Four genes encoding different type I signal peptidases are organized in a cluster in Streptomyces lividans TK21.
Microbiology (Reading). 1999 Sep;145 ( Pt 9):2255-2263. doi: 10.1099/00221287-145-9-2255.
10
The Sip(Sli) gene of Streptomyces lividans TK24 specifies an unusual signal peptidase with a putative C-terminal transmembrane anchor.
DNA Seq. 1998;9(2):79-88. doi: 10.3109/10425179809086432.
引用本文的文献
1
Secretory expression of recombinant small laccase genes in Gram-positive bacteria.
Microb Cell Fact. 2023 Apr 17;22(1):72. doi: 10.1186/s12934-023-02075-5.
2
Functional identification of a FKBP-like protein involved in the folding of overproduced secreted proteins.
Open Biol. 2019 Oct 31;9(10):190201. doi: 10.1098/rsob.190201. Epub 2019 Oct 30.
3
Four thiol-oxidoreductases involved in the formation of disulphide bonds in the Streptomyces lividans TK21 secretory proteins.
Microb Cell Fact. 2019 Jul 25;18(1):126. doi: 10.1186/s12934-019-1175-0.
4
The Cellular Mechanisms that Ensure an Efficient Secretion in Streptomyces.
Antibiotics (Basel). 2018 Apr 14;7(2):33. doi: 10.3390/antibiotics7020033.
5
The Three Streptomyces lividans HtrA-Like Proteases Involved in the Secretion Stress Response Act in a Cooperative Manner.
PLoS One. 2016 Dec 15;11(12):e0168112. doi: 10.1371/journal.pone.0168112. eCollection 2016.
6
Exploring the Feasibility of the Sec Route to Secrete Proteins Using the Tat Route in Streptomyces lividans.
Mol Biotechnol. 2015 Oct;57(10):931-8. doi: 10.1007/s12033-015-9883-0.
7
Overproduction of a Model Sec- and Tat-Dependent Secretory Protein Elicits Different Cellular Responses in Streptomyces lividans.
PLoS One. 2015 Jul 22;10(7):e0133645. doi: 10.1371/journal.pone.0133645. eCollection 2015.
8
A novel two-component system involved in secretion stress response in Streptomyces lividans.
PLoS One. 2012;7(11):e48987. doi: 10.1371/journal.pone.0048987. Epub 2012 Nov 14.
9
Pseudomonas aeruginosa possesses two putative type I signal peptidases, LepB and PA1303, each with distinct roles in physiology and virulence.
J Bacteriol. 2012 Sep;194(17):4521-36. doi: 10.1128/JB.06678-11. Epub 2012 Jun 22.
10
A novel two-component system involved in the transition to secondary metabolism in Streptomyces coelicolor.
PLoS One. 2012;7(2):e31760. doi: 10.1371/journal.pone.0031760. Epub 2012 Feb 9.
本文引用的文献
1
Taking a genetic scalpel to the Streptomyces colony.
Microbiology (Reading). 1998 Jun;144(6):1465-1478. doi: 10.1099/00221287-144-6-1465.
2
Functional analysis of the Streptomyces lividans type I signal peptidases.
Arch Microbiol. 2001 Nov;176(5):377-80. doi: 10.1007/s002030100335.
3
Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1.
Science. 1999 Nov 19;286(5444):1571-7. doi: 10.1126/science.286.5444.1571.
4
Control of synthesis and secretion of the Bacillus subtilis protein YqxM.
J Bacteriol. 1999 Nov;181(22):7065-9. doi: 10.1128/JB.181.22.7065-7069.1999.
5
Four genes encoding different type I signal peptidases are organized in a cluster in Streptomyces lividans TK21.
Microbiology (Reading). 1999 Sep;145 ( Pt 9):2255-2263. doi: 10.1099/00221287-145-9-2255.
6
Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.
Genes Dev. 1998 Aug 1;12(15):2318-31. doi: 10.1101/gad.12.15.2318.
7
The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.
Nature. 1997 Nov 27;390(6658):364-70. doi: 10.1038/37052.
8
Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes.
J Biol Chem. 1997 Oct 10;272(41):25983-92. doi: 10.1074/jbc.272.41.25983.
9
Heterologous biopharmaceutical protein expression in Streptomyces.
Trends Biotechnol. 1997 Aug;15(8):315-20. doi: 10.1016/s0167-7799(97)01062-7.
10
The chemistry and enzymology of the type I signal peptidases.
Protein Sci. 1997 Jun;6(6):1129-38. doi: 10.1002/pro.5560060601.
Zotero 插件