Alteration of T4 Lysozyme Structure by Second-site Reversion of Deleterious Mutations

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1998 Feb 12

PMID 9385644

Citations 15

Authors

A R Poteete

D Rennell

S E Bouvier

L W Hardy

Affiliations

Soon will be listed here.

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.

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