HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae

✍ Scribed by Noskov, V. N.; Staak, K.; Shcherbakova, P. V.; Kozmin, S. G.; Negishi, K.; Ono, B.-C.; Hayatsu, H.; Pavlov, Y. I.

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 923 KB
• Volume: 12
• Category: Article
• ISSN: 0749-503X
• DOI: 10.1002/(sici)1097-0061(199601)12:1<17::aid-yea875>3.0.co;2-i

✦ Synopsis

The haml mutant of yeast Saccharomyces cerevisiae is sensitive to the mutagenic and lethal effects of the base analog, 6-N-hydroxylaminopurine (HAP). We have isolated a clone from a centromere-plasmid-based genomic library complementing HAP sensitivity of the haml strain. After subcloning, a 3.4 kb functional fragment was sequenced.

It contained three open reading frames (ORFs) corresponding to proteins 353, 197 and 184 amino acids long. LEU2' disruptions of the promoter and N-terminal part of the gene coding 197 amino acids long protein led to moderate and strong sensitivity to HAP, respectively, and were allelic to the original haml-1 mutation. Thus this ORF represents the HAMI gene. The deduced amino acid sequence of HAM1 protein was not similar to any protein sequence of the SwissProt database. The H A M l gene was localized on the right arm of chromosome X between cdc8 and cdcll. Spontaneous mutagenesis was not affected by the haml::LEU2 disruption mutation.