The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence

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OriginalspracheEnglisch
Seiten (von - bis)90-94
Seitenumfang5
FachzeitschriftFEBS letters
Jahrgang347
Ausgabenummer1
PublikationsstatusVeröffentlicht - 20 Juni 1994
Extern publiziertJa

Abstract

The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.

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The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence. / Braun, Hans Peter; Jänsch, Lothar; Kruft, Volker et al.
in: FEBS letters, Jahrgang 347, Nr. 1, 20.06.1994, S. 90-94.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Braun HP, Jänsch L, Kruft V, Schmitza UK. The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence. FEBS letters. 1994 Jun 20;347(1):90-94. doi: 10.1016/0014-5793(94)00515-X
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abstract = "The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.",
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T1 - The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence

AU - Braun, Hans Peter

AU - Jänsch, Lothar

AU - Kruft, Volker

AU - Schmitza, Udo K.

N1 - Funding information: assistance. This work was supported by the Deutsche Forschungsge-meinsehaft, Grant Schm. 698/2.

PY - 1994/6/20

Y1 - 1994/6/20

N2 - The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.

AB - The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source reveals that it has a surplus of basic residues in potato. While the overall identity between the deduced amino acid sequence of the potato 'Hinge' protein and the proteins from yeast and bovine is in the range of 40%, the characteristic acidic domain is lacking. Therefore the numerous theories on the function of the mitochondrial 'Hinge' protein seem not to apply for the protein from potato. Also the atypical acidic presequence of the 'Hinge' protein from fungi and mammals is absent as revealed by N-terminal sequencing of the isolated potato 'Hinge' protein. Functional implications of these results for the 'Hinge' proteins from other organisms are discussed.

KW - 'Hinge' protein

KW - Cytochrome c reductase

KW - Mitochondrion

KW - Protein import

KW - Respiratory chain

KW - Solanum tuberosum

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