Document Detail


F-actin is a substrate for protealysin, a metalloprotease of invasive Serratia proteamaculans.
MedLine Citation:
PMID:  22077798     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Homologous bacterial metalloproteases ECP32/grimelysin from Serratia grimesii and protealysin from Serratia proteamaculans are involved in the invasion of those non-pathogenic bacteria in eukaryotic cells and are suggested to translocate into the cytoplasm (Bozhokina et al., Cell Biol. Int. 35, 111-118, 2011). The proteases have been characterized as actin-hydrolyzing enzymes with a narrow specificity toward intact cell proteins. However, neither cleavage of F-actin, that is the main actin species in the cell, nor the properties of the cleaved F-actin have been previously investigated. In this work, we revealed the presence of protealysin in the cytoplasm of 3T3-SV40 cells infected with S. proteamaculans or recombinant E. coli expressing the protealysin gene. We also show for the first time that purified protealysin and the lysates of the recombinant E. coli producing protealysin cleave 20-40% of F-actin. The cleavage limited predominantly to the bond Gly42-Val43 efficiently increases the steady-state ATPase activity (dynamics) of F-actin. AlF(4) (-) abolishes this effect and promotes the nucleation of protealysin-cleaved Mg-G-actin even in the absence of 0.1 M KCl, likely due to the stabilization of lateral intermonomer contacts of actin subunits. Our results suggest that F-actin can be a target for protealysin upon its translocation into the host cell. Structured digital abstract protealysin cleaves Actin by protease assay (View interaction).
Authors:
Olga Tsaplina; Tatiana Efremova; Ilya Demidyuk; Sofia Khaitlina
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-11
Journal Detail:
Title:  The FEBS journal     Volume:  -     ISSN:  1742-4658     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Journal compilation © 2011 Federation of European Biochemical Societies.
Affiliation:
Institute of Cytology, RAS, Tikhoretsky av. 4, 194064 St. Petersburg, Russia Institute of Molecular Genetics, RAS, Kurchatov sq. 2, 123182 Moscow, Russia.
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