Document Detail

Genetic analysis of yeast iso-1-cytochrome c structural requirements: suppression of Gly6 replacements by an Asn52----Ile replacement.
MedLine Citation:
PMID:  1654826     Owner:  NLM     Status:  MEDLINE    
Gly6 (vertebrate numbering system) is an evolutionarily invariant amino acid located in an electron-dense region of cytochrome c. Serine, cysteine, and aspartic acid replacements of Gly6 abolished yeast iso-1-cytochrome c function, presumably by destabilizing the mature forms of the altered proteins (1). Here we report that genetic reversion analysis of these mutants has uncovered a single base-pair substitution, encoding an Asn52----Ile replacement, that suppresses all three position 6 defects, as well as a Gly6....Gly29----Ser6....Ser29 double replacement. In each case the suppressor restored at least partial function to the altered iso-1-cytochromes c, with the Sera6....Ile52 protein being nearly indistinguishable from the normal protein. The suppressor also affected otherwise normal iso-1-cytochrome c, enhancing the in vivo amount of the protein by about 20%. While this work was in progress, Das et al. (1989, Proc. Natl. Acad. Sci. USA 86, 496-499) uncovered Ile52 as a suppressor of single Gly29 and His33 replacements in iso-1-cytochrome c. The ability of Ile52 to suppress amino acid replacements at three different sites, and its effect in isolation from the primary mutations, defines Ile52 as a global suppressor of specific iso-1-cytochrome c structural defects. These data suggest that position 52 plays a critical role in the folding and/or stability of iso-1-cytochrome c.
R W Berroteran; M Hampsey
Related Documents :
23153376 - Duplex destabilization by four ribosomal dead-box proteins.
9156316 - Characterisation of five missense mutations in the cystathionine beta-synthase gene fro...
24825296 - The cell wall pectic polymer rhamnogalacturonan-ii is required for proper pollen tube e...
24438646 - Regulation of protein degradation pathways by amino acids and insulin in skeletal muscl...
25063806 - The n- and c-terminal domains of tomosyn play distinct roles in snare binding and fusio...
1354626 - Streptomyces lividans possesses a groel-like chaperonin.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  288     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1991 Jul 
Date Detail:
Created Date:  1991-10-24     Completed Date:  1991-10-24     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  261-9     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, Shreveport 71130.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Base Sequence
Cloning, Molecular
Cytochrome c Group / chemistry,  genetics*
Cytochromes c*
DNA Mutational Analysis
DNA, Fungal / genetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Conformation
Saccharomyces cerevisiae / enzymology*,  genetics
Saccharomyces cerevisiae Proteins*
Suppression, Genetic
Grant Support
Reg. No./Substance:
0/CYC1 protein, S cerevisiae; 0/Cytochrome c Group; 0/DNA, Fungal; 0/Saccharomyces cerevisiae Proteins; 9007-43-6/Cytochromes c

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Activation of phosphoinositide-specific phospholipase C delta from rat liver by polyamines and basic...
Next Document:  5,5-dimethyl-1-pyrroline-N-oxide alone enhances the spontaneous superoxide generation by primaquine.