Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein.
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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 ...
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Temperature-sensitive folding mutations (tsf) of the thermostable P22 tailspike protein prevent the mutant polypeptide chain from reaching the native state at the higher end of the temperature range of bacterial growth (37-42 degrees C). At lower temperatures the mutant polypeptide chains fold and associate into native proteins. The melting temperatures of the purified native forms of seven dif...
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The amino acid sequence of a polypeptide defines both the folding pathway and the final three-dimensional structure of a protein. Eighteen amino acid substitutions have been identified in bacteriophage P22 coat protein that are defective in folding and cause their folding intermediates to be substrates for GroEL and GroES. These temperature-sensitive folding (tsf) substitutions identify amino a...
متن کاملGenetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.
Temperature-sensitive mutations fall into two general classes: those generating thermolabile proteins; and those generating defects in protein synthesis, folding or assembly. Temperature-sensitive mutations at 17 sites in the gene for the coat protein of Phage P22 are of the latter class, preventing the productive folding of the polypeptide chain at restrictive temperature. We show here that, t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)57320-3