Specific mitochondrial proteins in pollen: presence of an additional ATP synthase beta subunit

A protocol was designed to obtain a pure fraction of pollen mitochondria from the diploid species Nicotiana sylvestris, the female parent of the allotetraploid Nicotiana tabacum. Most organelles were morphologically intact and able to perform in organello mitochondrial (mt) protein synthesis. As rev...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-07, Vol.90 (13), p.5934-5938
Main Authors: De Paepe, R, Forchioni, A, Chetrit, P, Vedel, F
Format: Article
Language:English
Subjects:
Adenosine triphosphatases
ADENOSINE TRIPHOSPHATE
ADENOSINTRIFOSFATO
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Anthers
Biological and medical sciences
Cell Fractionation
Corn
ELECTROFORESIS
ELECTROPHORESE
Electrophoresis, Gel, Two-Dimensional
Fundamental and applied biological sciences. Psychology
GAMETOGENESE
GAMETOGENESIS
Gels
LIASAS
LYASE
Microspores
Microsporocytes
Miscellaneous
Mitochondria
Mitochondria - enzymology
MITOCHONDRIE
MITOCONDRIA
Molecular Sequence Data
NICOTIANA
Nicotiana - enzymology
Nicotiana - ultrastructure
Plants, Toxic
POLEN
POLLEN
Pollen - enzymology
Pollen - ultrastructure
Proteins
Proton-Translocating ATPases - analysis
Proton-Translocating ATPases - chemistry
Proton-Translocating ATPases - genetics
Proton-Translocating ATPases - isolation & purification
SINTESIS DE PROTEINAS
Somatic cells
SYNTHESE PROTEIQUE
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Summary:A protocol was designed to obtain a pure fraction of pollen mitochondria from the diploid species Nicotiana sylvestris, the female parent of the allotetraploid Nicotiana tabacum. Most organelles were morphologically intact and able to perform in organello mitochondrial (mt) protein synthesis. As revealed by two-dimensional protein electrophoresis, numerous quantitative differences exist between leaf and pollen mt proteins. Moreover, additional mt polypeptides, named R (for reproductive), encoded by either nuclear or mitochondrial genes, are found in pollen. The most abundant R polypeptide, R1 (Mr 53,000, pI 5.6), is nuclearly encoded, is membrane bound, and cross-reacts with an antibody directed against the beta subunit of the mt ATP synthase (ATPase). N-terminal microsequence analysis showed that the two ATPase beta subunits present in leaves (P1 and P2) and the R1 pollen-specific subunit are encoded by distinct genes. A similar additional ATPase beta subunit was observed in pollen mitochondria from Petunia, suggesting that this polypeptide is of general importance for male gametophytic development in Solanaceaes
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.13.5934