PMC:4502370 / 38671-39559 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4502370","sourcedb":"PMC","sourceid":"4502370","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4502370","text":"Rpo26 mutations that separate rpo26Δ complementation and tgs1Δ suppression activities\nAs one might expect, the R79A, D145A, and E150A mutants that complemented rpo26∆ at 18° were also active in suppressing tgs1∆ (Figure 6C). Mutations E89A and R136A that unconditionally abolished rpo26∆ complementation also eliminated tgs1∆ suppression. The salient findings were that: (i) two other mutants, R135A and E124A, that were unconditionally defective in rpo26∆ complementation retained tgs1∆ suppressor activity and (ii) mutant R97A, which was inactive in rpo26∆ complementation at 18°, nonetheless complemented tgs1∆ growth at 18°. Thus, R135A, E124A, and R97A exemplify separation of function mutations that distinguish the global role of Rpo26 in transcription by all nuclear RNA polymerases from its particular ability to act as a dosage suppressor of the cold sensitivity of tgs1∆ cells.","divisions":[{"label":"title","span":{"begin":0,"end":85}}],"tracks":[]}