Literature DB >> 12169613

SipY Is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion.

Arantxa Palacín1, Víctor Parro, Nick Geukens, Jozef Anné, Rafael P Mellado.   

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.

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Year:  2002        PMID: 12169613      PMCID: PMC135301          DOI: 10.1128/JB.184.17.4875-4880.2002

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  30 in total

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Authors:  N Geukens; V Parro; L A Rivas; R P Mellado; J Anné
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Authors:  H Tjalsma; M A Noback; S Bron; G Venema; K Yamane; J M van Dijl
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3.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
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4.  Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.

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5.  Preparation of polyclonal antibodies.

Authors:  B S Dunbar; E D Schwoebel
Journal:  Methods Enzymol       Date:  1990       Impact factor: 1.600

6.  A morphological and genetic mapping study of white colony mutants of Streptomyces coelicolor.

Authors:  K F Chater
Journal:  J Gen Microbiol       Date:  1972-08

7.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

8.  Control of synthesis and secretion of the Bacillus subtilis protein YqxM.

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Authors:  C Yanisch-Perron; J Vieira; J Messing
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  9 in total

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2.  Pseudomonas aeruginosa possesses two putative type I signal peptidases, LepB and PA1303, each with distinct roles in physiology and virulence.

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Review 3.  Signal peptidase I: cleaving the way to mature proteins.

Authors:  Sarah M Auclair; Meera K Bhanu; Debra A Kendall
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4.  A novel two-component system involved in the transition to secondary metabolism in Streptomyces coelicolor.

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5.  Overproduction of a Model Sec- and Tat-Dependent Secretory Protein Elicits Different Cellular Responses in Streptomyces lividans.

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Journal:  PLoS One       Date:  2015-07-22       Impact factor: 3.240

6.  The Three Streptomyces lividans HtrA-Like Proteases Involved in the Secretion Stress Response Act in a Cooperative Manner.

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8.  A novel two-component system involved in secretion stress response in Streptomyces lividans.

Authors:  Sonia Gullón; Rebeca L Vicente; Rafael P Mellado
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9.  Functional identification of a Streptomyces lividans FKBP-like protein involved in the folding of overproduced secreted proteins.

Authors:  R L Vicente; S Marín; J R Valverde; C Palomino; R P Mellado; S Gullón
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  9 in total

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