Abstract
THE respiratory chain complexes of mitochondria consist of many different subunits, of which only a few partake directly in electron transport. The functions of the subunits that do not contain prosthetic groups are largely unknown1. The cytochrome reductase complex of Neurospora crassa , for example, consists of nine different subunits2, of which the peripheral membrane proteins I and II (ref. 3) that are located on the matrix side of the mitochondrial inner membrane4 are the largest subunits devoid of redox centres. Significantly, a cytochrome reductase fraction lacking these two subunits was inactive in electron transfer5, and in yeast mutants with defective genes for either of the two subunits, assembly of the reductase is disrupted6,7. Most mitochondrial proteins are imported into the mitochondrion as precursor proteins, and two proteins are necessary for cleaving their presequences8, namely the matrix processing peptidase (MPP) and the processing enhancing protein (PEP), the latter strongly stimulating the activity of the former9. Temperature-sensitive yeast mutants, which are affected in PEP or MPP, accumulate precursors at the non-permissive temperature10 –12. We report here that subunit I of the cytochrome reductase complex of N. crassa. is identical to PEP and that the protein is therefore bifunctional, participating in both electron transport and protein processing. The processing proteins and subunits I and II of cytochrome reductase can be grouped as members of the same protein family.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Hatefi, Y. A. Rev. Biochem. 54, 1015–1065 (1985).
Weiss, H. Curr. Topics Bioenerg. 15, 67–90 (1987).
Silman, H. J., Rieske, J. S., Lipton, S. H. & Baum, H. J. biol. Chem. 242, 4967–4875 (1967).
Karlsson, B., Hovmöller, S., Weiss, H. & Leonard, K. J. molec. Biol. 165, 287–302 (1983).
Linke, P. & Weiss, H. Meth. Enzym. 126, 201–211 (1984).
Tzagoloff, A., Wu, M. & Crivellone, M. J. biol. Chem. 261, 17163–17169 (1986).
Oudshoorn, P., van Steeg, H., Swinkels, B. W., Schoppink, P. & Grivell, L. A. Eur. J. Biochem. 163, 97–103 (1987).
Pfanner, N., Hartl, F. U. & Neupert, W. Eur. J. Biochem. 175, 205–212 (1988).
Hawlitschek, G., Schneider, H., Schmidt, B., Tropschug, M., Hartl, F. U. & Neupert, W. Cell 53, 795–806 (1988).
Yaffe, M. P., Otha, S. & Schatz, G. EMBO J. 4, 2069–2074 (1985).
Witte, C., Jensen, R. E., Yaffe, M. P. & Schatz, G. EMBO J. 7, 1439–1447 (1988).
Pollock, R. A., Hartl, F. U., Cheng, M. Y., Ostermann, J., Horwich, A. & Neupert, W. EMBO J. 7, 3493–3500 (1988).
Weiss, H. & Kolb, H. J. Eur. J. Biochem. 99, 139–149 (1979).
Teintze, M., Slaughter, M., Weiss, H. & Neupert, W. J. biol. Chem. 257, 10364–10371 (1982).
Viebrock, A., Perz, A. & Sebald, W. EMBO J. 1, 565–571 (1982).
Sachs, M. S., David, M., Werner, S. & Rajsshandary, U. L. J. biol. Chem. 261, 869–873 (1986).
Yang, M., Jensen, R. E., Yaffe, M. P., Oppliger, W. & Schatz, G. EMBO J. 7, 3857–3862 (1988).
Burnette, W. N. Analyt. Biochem. 112, 195–203 (1981).
Blake, M.S., Johnston, K. H., Russel-Jones, G. J. & Gotschlick, E. C. Analyt. Biochem. 136, 175–179 (1984).
Southern, E. J. molec. Biol. 98, 503–517 (1975).
Jensen, R. E. & Yaffe, M. P. EMBO J. 7, 3863–3871 (1988).
Kyte, J. & Doolittle, R. F. J. molec. Biol. 157, 105–132 (1982).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schulte, U., Arretz, M., Schneider, H. et al. A family of mitochondrial proteins involved in bioenergetics and biogenesis. Nature 339, 147–149 (1989). https://doi.org/10.1038/339147a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/339147a0
This article is cited by
-
Critical role of UQCRC1 in embryo survival, brain ischemic tolerance and normal cognition in mice
Cellular and Molecular Life Sciences (2019)
-
Mitochondrial and plastid evolution in eukaryotes: an outsiders' perspective
Nature Reviews Genetics (2009)
-
Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc 1 complex inSpinacia oleracea
Journal of Bioenergetics and Biomembranes (1996)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.