Amino acid replacements resulting from suppression and missense reversion of a chain-terminator mutation in Neurospora.

Abstract:

:The Neurospora crassa super-suppressor mutation, ssu-1, suppresses the auxotrophic phenotype of the mutant am(17) by inserting tyrosine at residue 313 of NADP-specific glutamate dehydrogenase, a position occupied in the wild type by glutamate. Two classes of am(17) revertants due to further mutation within the am gene have, respectively, tyrosine and leucine at residue 313. These replacements are consistent with a chain-terminating codon in am(17) of either the amber (UAG) or the ochre type (UAA), but are inconsistent with UGA. The Leu313 and Tyr313 variants of the enzyme have effective activity but are grossly different from the wild type in Michaelis constants (especially for ammonium) and heat stabilities at two different pH values. They show smaller but significant differences in these respects from each other.

journal_name

Genetics

journal_title

Genetics

authors

Seale TW,Brett M,Baron AJ,Fincham JR

subject

Has Abstract

pub_date

1977-06-01 00:00:00

pages

261-74

issue

2 Pt. 1

eissn

0016-6731

issn

1943-2631

journal_volume

86

pub_type

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