Mechanism of phage P22 tailspike protein folding mutations
نویسندگان
چکیده
منابع مشابه
Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein.
Temperature-sensitive folding (tsf) mutations in the gene for the thermostable P22 tailspike interfere with the polypeptide chain folding and association pathway at restrictive temperature without altering the thermostability of the protein once correctly folded and assembled at permissive temperature. Though the native proteins matured at permissive temperature are biologically active, many of...
متن کاملMolecular properties of global suppressors of temperature-sensitive folding mutations in P22 tailspike endorhamnosidase.
Two global suppressors (Val-331 greater than Ala and Ala-334 greater than Val) have been identified for temperature-sensitive folding (tsf) mutations in gene 9 of bacteriophage P22 (Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J., and King, J. (1991) Science 253, 54-58). We have introduced 19 different single amino acid substitutions at the two global suppressor sites independently ...
متن کاملStem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein
The P22 tailspike protein is an intensely studied protein whose structure and sequence has been described. However, a study, describing important protein interactions related to its function at the N-terminal domain, has been lacking. The P22 tailspike protein (TSP) consists of three identical polypeptide chains of 666aa. The first 108 of the 666aa in the P22 TSP form a trimeric N-terminal doma...
متن کاملCarbohydrate binding of Salmonella phage P22 tailspike protein and its role during host cell infection.
TSPs (tailspike proteins) are essential infection organelles of bacteriophage P22. Upon infection, P22TSP binds to and cleaves the O-antigen moiety of the LPS (lipopolysaccharide) of its Salmonella host. To elucidate the role of TSP during infection, we have studied binding to oligosaccharides and polysaccharides of Salmonella enterica Typhimurium and Enteritidis in vitro. P22TSP is a trimeric ...
متن کاملInteractions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro.
Because efficient folding in vivo and reconstitution in vitro of phage P22 tailspike protein is temperature-sensitive, and because a chaperone function of the GroE proteins for tailspike folding in vivo has been suggested by genetic observations, the interactions of purified Escherichia coli GroE proteins with phage P22 tailspikes during refolding in vitro were investigated. At elevated tempera...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1993
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560021109