Biochemical and genetic characterization of the structure of yeast ornithine decarboxylase.

Abstract:

:The ornithine decarboxylase gene of S. cerevisiae encodes a predicted protein of approximately 53 kD highly homologous with the ornithine decarboxylase of other species. However, the native enzyme has been reported as an 86 kD protein. Our molecular sieve analysis indicated a Mr = 110,000 for the native enzyme. SDS-PAGE analysis of [H3]-alpha-difluoromethylornithine labelled enzyme demonstrated a subunit Mr of approximately 50 kD and suggested the native enzyme is a dimer. Genetic analyses support this conclusion. The complementary, ornithine decarboxylase deficient mutations spe 1A and spe 1B were mapped to the enzyme structural gene by linkage analysis and gene conversion mapping. This demonstrated that the mutations exhibit intragenic complementation which suggests protein-protein interactions and an oligomeric structure for the yeast enzyme. We conclude that yeast ornithine decarboxylase is a dimeric enzyme of 53 kD subunits.

authors

Fonzi WA

doi

10.1016/0006-291x(89)90831-0

subject

Has Abstract

pub_date

1989-08-15 00:00:00

pages

1409-16

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)90831-0

journal_volume

162

pub_type

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