Diminished Degradation of Yeast Cytochrome C by Interactions with Its Physiological Partners

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1995 Apr 25

PMID 7731975

Citations 6

Authors

D A Pearce

F Sherman

Affiliations

Soon will be listed here.

Abstract

The level and structure of yeast iso-1-cytochrome c and iso-2-cytochrome c, encoded by the nuclear genes CYC1 and CYC7, respectively, are normally not altered in rho- mutants, which completely lack the cytochromes a.a3 subunits and cytochrome b that are encoded by mitochondrial DNA. In contrast, iso-cytochromes c containing the amino acid change Thr-78-->Ile (T78I) were observed at the normal or near-normal wild-type level in rho+ strains but were completely absent in rho- mutants. We have demonstrated with the "global" suppressor mutation Asn-52-->Ile and by pulse-chase labeling that the T78I iso-1-cytochrome c undergoes rapid cellular degradation in rho- mutants. Furthermore, specific mutations revealed that the deficiency of T78I iso-1 cytochrome c can be caused by the lack of cytochrome a.a3 or cytochrome c1, but not by the lack of cytochrome b. Thus, this and certain other, but not all, labile forms of cytochrome c are protected from degradation by the interaction with its physiological partners.

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References

Sherman F, Taber H, Campbell W . Genetic determination of iso-cytochromes c in yeast. J Mol Biol. 1965; 13(1):21-39. DOI: 10.1016/s0022-2836(65)80077-8. View

Reilly C, Sherman R . GLUCOSE REPRESSION OF CYTOCHROME A-SYNTHESIS IN CYTOCHROME-DEFICIENT MUTANTS OF YEAST. Biochim Biophys Acta. 1965; 95:640-51. DOI: 10.1016/0005-2787(65)90518-6. View

Sanders H, Mied P, Briquet M, Hernandez-Rodriguez J, Gottal R, Mattoon J . Regulation of mitochondrial biogenesis: yeast mutants deficient in synthesis of delta-aminolevulinic acid. J Mol Biol. 1973; 80(1):17-39. DOI: 10.1016/0022-2836(73)90231-3. View

Sherman F, Stewart J, Jackson M, Gilmore R, Parker J . Mutants of yeast defective in iso-1-cytochrome c. Genetics. 1974; 77(2):255-84. PMC: 1213128. DOI: 10.1093/genetics/77.2.255. View

Downie J, Stewart J, Brockman N, Schweingruber A, Sherman F . Structural gene for yeast iso-2-cytochrome c. J Mol Biol. 1977; 113(2):369-84. DOI: 10.1016/0022-2836(77)90147-4. View

SANGER F, Nicklen S, Coulson A . DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977; 74(12):5463-7. PMC: 431765. DOI: 10.1073/pnas.74.12.5463. View

Downie J, Stewart J, Sherman F . Yeast mutants defective in iso-2-cytochrome c. J Mol Biol. 1977; 117(2):369-86. DOI: 10.1016/0022-2836(77)90133-4. View

Lancashire W, Mattoon J . Genetic manipulation of a latent defect in yeast cytochrome biosynthesis utilizing cytoduction. Biochem Biophys Res Commun. 1979; 90(3):801-9. DOI: 10.1016/0006-291x(79)91899-0. View

McKnight G, Cardillo T, Sherman F . An extensive deletion causing overproduction of yeast iso-2-cytochrome c. Cell. 1981; 25(2):409-19. DOI: 10.1016/0092-8674(81)90059-3. View

10.

Matner R, Sherman F . Differential accumulation of two apo-iso-cytochromes c in processing mutants of yeast. J Biol Chem. 1982; 257(16):9811-21. View

11.

Reid G . Pulse labeling of yeast cells and spheroplasts. Methods Enzymol. 1983; 97:324-9. DOI: 10.1016/0076-6879(83)97144-6. View

12.

Yaffe M, Schatz G . Two nuclear mutations that block mitochondrial protein import in yeast. Proc Natl Acad Sci U S A. 1984; 81(15):4819-23. PMC: 391582. DOI: 10.1073/pnas.81.15.4819. View

13.

Stueber D, Ibrahimi I, Cutler D, Dobberstein B, Bujard H . A novel in vitro transcription-translation system: accurate and efficient synthesis of single proteins from cloned DNA sequences. EMBO J. 1984; 3(13):3143-8. PMC: 557830. DOI: 10.1002/j.1460-2075.1984.tb02271.x. View

14.

Dumont M, Ernst J, Hampsey D, Sherman F . Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae. EMBO J. 1987; 6(1):235-41. PMC: 553382. DOI: 10.1002/j.1460-2075.1987.tb04744.x. View

15.

Maicas E, Pluthero F, Friesen J . The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay. Mol Cell Biol. 1988; 8(1):169-75. PMC: 363097. DOI: 10.1128/mcb.8.1.169-175.1988. View

16.

Schagger H, von Jagow G . Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987; 166(2):368-79. DOI: 10.1016/0003-2697(87)90587-2. View

17.

elBaradi T, van der Sande C, Mager W, Raue H, Planta R . The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein. Curr Genet. 1986; 10(10):733-9. DOI: 10.1007/BF00405095. View

18.

Tsay Y, Thompson J, Rotenberg M, Larkin J, Woolford Jr J . Ribosomal protein synthesis is not regulated at the translational level in Saccharomyces cerevisiae: balanced accumulation of ribosomal proteins L16 and rp59 is mediated by turnover of excess protein. Genes Dev. 1988; 2(6):664-76. DOI: 10.1101/gad.2.6.664. View

19.

Das G, Hickey D, McLendon D, McLendon G, Sherman F . Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57. Proc Natl Acad Sci U S A. 1989; 86(2):496-9. PMC: 286497. DOI: 10.1073/pnas.86.2.496. View

20.

Dumont M, Mathews A, Nall B, Baim S, Eustice D, Sherman F . Differential stability of two apo-isocytochromes c in the yeast Saccharomyces cerevisiae. J Biol Chem. 1990; 265(5):2733-9. View