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Digitale Medien

Expression of the Saccharomyces cerevisiae CYT2 gene, encoding cytochrome c1 heme lyase (1994)

Zollner, Alfred ; Rödel, Gerhard ; Haid, Albert

Springer

Current genetics 25 (1994), S. 291-298

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ISSN: 1432-0983

Schlagwort(e): Cytochrome c 1 ; Cytochrome c 1 heme lyase ; GRF2p ; Glucose repression ; HAPp ; Saccharomyces cerevisiae

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract In this paper we examine the expression of the Saccharomyces cerevisiae CYT2 gene, which encodes cytochrome c 1 heme lyase. This enzyme is required for covalent attachment of heme to apocytochrome c 1, a subunit of the mitochondrial respiratory chain. Transcription of the 1-kb CYT2 mRNA initiates at four prominent sites at a distance of 52–225 bp in front of the AUG start codon. The level of CYT2 mRNA is not influenced by the presence or absence of oxygen or of heme, but it is subject to carbonsource control. The concentration of the CYT2 mRNA is significantly reduced in glucose-grown cells as compared to cells grown under non-repressing conditions. Neither the HAPp activator proteins nor MIG1p, a repressor protein involved in glucose repression, seem to mediate this effect.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00351480

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Digitale Medien

Mutation of a highly conserved base in the yeast mitochondrial 21S rRNA restricts ribosomal frameshifting (1995)

Weiss-Brummer, Brigitte ; Zollner, Alfred ; Haid, Albert ; [weitere]

Springer

Molecular genetics and genomics 248 (1995), S. 207-216

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ISSN: 1617-4623

Schlagwort(e): Chloramphenicol resistance ; frameshifting Mitochondria ; 21S rRNA ; Yeast

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract A mutation shown to cause resistance to chloramphenicol inSaccharomyces cerevisiae was mapped to the central loop in domain V of the yeast mitochondrial 21S rRNA. The mutant 21S rRNA has a base pair exchange from U2677 (corresponding to U2504 inEscherichia coli) to C2677, which significantly reduces rightward frameshifting at a UU UUU UCC A site in a + 1 U mutant. There is evidence to suggest that this reduction also applies to leftward frameshifting at the same site in a − 1 U mutant. The mutation did not increase the rate of misreading of a number of mitochondrial missense, nonsense or frameshift (of both signs) mutations, and did not adversely affect the synthesis of wild-type mitochondrial gene products. It is suggested here that ribosomes bearing either the C2677 mutation or its wild-type allele may behave identically during normal decoding and only differ at sites where a ribosomal stall, by permitting non-standard decoding, differentially affects the normal interaction of tRNAs with the chloramphenicol resistant domain V. Chloramphenicol-resistant mutations mapping at two other sites in domain V are described. These mutations had no effect on frameshifting.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF02190802

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