The 4-kDa nuclear-encoded PetM polypeptide of the chloroplast cytochrome b6f complex. Nucleic acid and protein sequences, targeting signals, transmembrane topology. [Erratum: Oct 4, 1996, v. 271 (40), p. 25058.]

The 4-kDa subunit of cytochrome b6f complex encoded by the nuclear PetM gene in Chlamydomonas reinhardtii has been characterized. 38 of the 39 residues of the mature protein have been established by Edman degradation, a cDNA clone encoding the complete precursor has been isolated and sequenced, and...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-05, Vol.271 (18), p.10667-10671
Main Authors: Vitry, C. de (CNRS/URA, Paris, France.), Breyton, C, Pierre, Y, Popot, J.L
Format: Article
Language:English
Subjects:
ADN
Amino Acid Sequence
Base Sequence
Biochemistry, Molecular Biology
Cell Membrane
Cell Membrane - metabolism
CHLAMYDOMONAS REINHARDTII
CHLOROPLASTE
Chloroplasts
Chloroplasts - enzymology
CITOCROMOS
CLONACION
CLONAGE
CLOROPLASTO
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
CYTOCHROME
Cytochrome b Group
Cytochrome b Group - chemistry
Cytochrome b6f Complex
DNA, Complementary
Life Sciences
Molecular Sequence Data
Nuclear Proteins
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
PEPTIDE
PEPTIDOS
Plant Proteins
Protein Conformation
SECUENCIA NUCLEOTIDICA
SEQUENCE NUCLEOTIDIQUE
Structural Biology
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Summary:The 4-kDa subunit of cytochrome b6f complex encoded by the nuclear PetM gene in Chlamydomonas reinhardtii has been characterized. 38 of the 39 residues of the mature protein have been established by Edman degradation, a cDNA clone encoding the complete precursor has been isolated and sequenced, and a 0.6-kb transcript detected. The deduced amino acid sequence of the precursor includes an N-terminal transit peptide of 60 amino acids with stromal targeting features. Examination of the sequence suggests that PetM spans the membrane as a single transmembrane alpha-helix, which is supported by its non-extractability following dissociating treatments. When PetM and PetG, another small subunit of the b6f complex, are folded into alpha-helices, an array of identical residues becomes apparent. Proteolysis data, charge distribution, and homology with PetG are consistent with a lumenal localization of the N terminus of PetM
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.18.10667