Reference : Thermosensitive mutations affecting ribonucleic acid polymerases in Saccharomyces cer...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/79981
Thermosensitive mutations affecting ribonucleic acid polymerases in Saccharomyces cerevisiae
English
Thonart, Philippe mailto [Université de Liège - ULg > Département des sciences de la vie > Biochimie et microbiologie industrielles - Bio-industries >]
Bechet, Jacques [ > > ]
Hilger, François [ > > ]
Burny, Arsène [ > > ]
Jan-1976
Journal of Bacteriology
American Society for Microbiology (ASM)
125
1
25-32
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] Among 150 temperature-sensitive Saccharomyces cerevisiae mutants which we have isolated, 15 are specifically affected in ribonucleic acid (RNA) synthesis. Four of these mutants exhibit particularly drastic changes and were chosen for a more detailed study. In these four mutants, RNA synthesis is immediately blocked after a shift at the nonpermissive temperature (37 C), protein synthesis decays at a rate compatible with messenger RNA half-life, and deoxyribonucleic
acid synthesis increases by about 40%. All the mutations display a recessive phenotype. The segregation of the four allelic pairs ts-/ts+ in diploids is mendelian, and the four mutants belong to three complementation groups. The elution patterns (diethylaminoethyl-Sephadex) of the three RNA polymerases of the mutants grown at 37 C for 3.5 h show very low residual activities. The in vitro thermodenaturation confirms the in vivo results; the half-lives of the mutant
activities at 45 C are 10 times smaller than those of the wild-type enzymes. Polyacrylamide gel electrophoresis shows that the synthesis of all species of RNA is thermosensitive. The existence of three distinct genes, which are each indispensable for the activity of the three RNA polymerases in vivo as well as in vitro, strongly favors the hypothesis of three common subunits in the three RNA polymerases.
http://hdl.handle.net/2268/79981

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