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Alteration of T4 lysozyme structure by second‐site reversion of deleterious mutations
Author(s) -
Poteete Anthony R.,
Rennell Dale,
Bouvier Suzanne E.,
Hardy Larry W.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560061115
Subject(s) - lysozyme , reversion , mutant , protein primary structure , mutation , genetics , primary (astronomy) , point mutation , biology , chemistry , active site , function (biology) , biochemistry , enzyme , peptide sequence , gene , phenotype , physics , astronomy
Abstract Mutations that suppress the defects introduced into T4 lysozyme by single amino acid substitutions were isolated and characterized. Among 53 primary sites surveyed, 8 yielded second‐site revertants; a total of 18 different mutants were obtained. Most of the restorative mutations exerted global effects, generally increasing lysozyme function in a number of primary mutant contexts. Six of them were more specific, suppressing only certain specific deleterious primary substitutions, or diminishing the function of lysozymes bearing otherwise nondeleterious primary substitutions. Some variants of proteins bearing primary substitutions at the positions of Asp 20 and Ala 98 are inferred to have significantly altered structures.