John W. Stewart

TL;DR: The result with the mutationally altered iso‐1‐cytochromes c and the results from published sequences of other proteins from a wide range of prokaryotes and eukaryotes suggest that the aminopeptidase usually cleaves amino‐terminal methionine when it precedes residues of alanine, cysteine, glycine, proline, serine, threonine and valine but not when it follows residues of arginine, as

TL;DR: Yeast contains acetyltransferases that acetylates these mutant forms of iso-1-cytochromes c because their amino-terminal regions resemble the amino- terminal regions of natural occurring proteins which are normally acetylated.

TL;DR: It is suggested that the predominant means for abolishing iso-1-cytochrome c by mutations are either through a complete loss, such as produced by chain terminating codons, or impairments through drastic changes of tertiary structure which lead to instability and thermolability.

TL;DR: A benzidine-H2O2 staining procedure and genetic tests were used for the detection of cytochrome c-deficient mutants of the cy1, cy2, cy3, cy4, and cy6 loci and it was revealed that all of the revertants from eight of the Cy1 mutants apparently contained normal iso-1-cy tochrome c, while a revertant which contained an altered protein was obtained from each of the other seven cy1 mutants.

TL;DR: These experiments show that the RAD6+ locus is intimately concerned with error-prone repair, and suggest that excision repair is substantially error-free, as well as suggesting that excisions are more sensitive to the lethal effects of both ultraviolet and X-irradiation.