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Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis
Author(s) -
Escutia Marta R.,
Val Gema,
Palacín Arantxa,
Geukens Nick,
Anné Jozef,
Mellado Rafael P.
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500927
Subject(s) - signal peptide , signal peptidase , extracellular , biology , complementation , secretion , proteome , protein fragment complementation assay , biochemistry , secretory protein , gene , peptide sequence , phenotype
The developmentally complex bacterium Streptomyces lividans has the ability to produce and secrete a significant amount of protein and possesses four different type I signal peptidase genes ( sipW , sipX , sipY and sipZ ) that are unusually clustered in its chromosome. 2‐DE and subsequent MS of extracellular proteins showed that proteins with typical export signals for type I and type II signal peptidases are the main components of the S. lividans secretome. Secretion of extracellular proteins is severely reduced in a strain deficient in the major type I signal peptidase (SipY). This deficiency was efficiently compensated by complementation with any of the other three signal peptidases as deduced from a comparison of the corresponding 2‐D PAGE patterns with that of the wild‐type strain.