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Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae.

Abstract：

:We examined folding and secretion of human lysozyme using four mutants each lacking two cysteines expressed in a yeast secretion system. Our results have revealed that the formation of the disulfide bond Cys6/Cys128 in human lysozyme is a prerequisite for correct folding in vivo in yeast. Substitution of Ala for Cys77 and Cys95 gave eight-fold greater secretion of a molecule with almost the same specific activity as that of the native enzyme. Substitutions of the other cysteines gave molecules that were secreted at a lower rate and had lower specific activities than the native enzyme. These are the first findings that the individual disulfide bonds of human lysozyme have different functions in folding and secretion in vivo.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Taniyama Y,Yamamoto Y,Nakao M,Kikuchi M,Ikehara M

doi

10.1016/s0006-291x(88)80377-2

subject

Has Abstract

pub_date

1988-05-16 00:00:00

pages

962-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80377-2

journal_volume

152

pub_type

杂志文章

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