Role of DegP for two-partner secretion inBordetella
نویسندگان
چکیده
منابع مشابه
functional study of p0 proteins of two cereal yellow dwarf viruses (cydv-rpv and cydv-rps) and identification of their cellular partner
نقش سرکوبگری پروتئین p0 در دو پولروویروس کوتولگی زردی غلات cydv-rpv) و (cydv-rps، متفاوت در شدت بیماریزایی، مورد مطالعه قرار گرفت. نتایج نشان داد که هر دو پروتئین p0 p0cy-rpv) و (p0cy-rps قادر به سرکوب خاموشی آر ان ای ایجاد شده توسط ترادف های تراژن سنس و تکرار معکوس در n. benthamiana هستند. نشان داده شد که هر دو پروتئین p0 می توانند تخریب پروتئین argonaute-1 را تسهیل کنند. علاوه بر این، تمایل م...
Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions
Initially identified in pathogenic Gram-negative bacteria, the two-partner secretion (TPS) pathway, also known as Type Vb secretion, mediates the translocation across the outer membrane of large effector proteins involved in interactions between these pathogens and their hosts. More recently, distinct TPS systems have been shown to secrete toxic effector domains that participate in inter-bacter...
متن کاملThe crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway.
Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping cough agent Bordetella pertussis, is one of the most efficiently secreted proteins in Gram-negative bacteria. FHA is secreted by means of the two-partner secretion (TPS) pathway. Several important human, animal, and plant pathogens also secrete adhesins and other virulence factors by using this mode of secretion. A TPS s...
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objective: acinetobacter baumannii (a. baumannii) has a good potential to colonize on various surfaces. as a virulence factor, adhesion to surfaces is the first step in colonization. the two-partner secretion system (tps) proteins are key factors for bacterial attachment. the purpose of this study is to identify and study the role of this family of proteins in adhesion of a. baumannii to human ...
متن کاملRole of the PDZ domains in Escherichia coli DegP protein.
PDZ domains are modular protein interaction domains that are present in metazoans and bacteria. These domains possess unique structural features that allow them to interact with the C-terminal residues of their ligands. The Escherichia coli essential periplasmic protein DegP contains two PDZ domains attached to the C-terminal end of the protease domain. In this study we examined the role of eac...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2009
ISSN: 0950-382X,1365-2958
DOI: 10.1111/j.1365-2958.2009.06860.x