Identification of a novel isoform of the chloroplast-coupling factor alpha-subunit

Studies were conducted to identify a 64-kD thylakoid membrane protein of unknown function. The protein was extracted from chloroplast thylakoids under low ionic strength conditions and purified to homogeneity by preparative sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Four peptides gene...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1998-02, Vol.116 (2), p.703-708
Main Authors: Burkey, K.O. (USDA-ARS, North Carolina State University, Raleigh, NC.), Mathis, J.N
Format: Article
Language:English
Subjects:
Acclimatization
Amino Acid Sequence
AMINO ACID SEQUENCES
Barley
Biological and medical sciences
Cell Biology and Signal Transduction
Cell structures and functions
CHEMICAL COMPOSITION
Chloroplast, photosynthetic membrane and photosynthesis
CHLOROPLASTE
CHLOROPLASTS
CLOROPLASTO
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Gels
Hordeum - enzymology
Hordeum - growth & development
HORDEUM VULGARE
Immunochemistry
Irradiance
Metabolism
Molecular and cellular biology
MOLECULAR SEQUENCE DATA
Peas
Photosynthesis, respiration. Anabolism, catabolism
Plant physiology and development
PLANT PROTEINS
Plants
Protein isoforms
PROTEINAS
PROTEINE
PROTEINS
Proton-Translocating ATPases - chemistry
Proton-Translocating ATPases - isolation & purification
PURIFICACION
PURIFICATION
THYLAKOIDE
THYLAKOIDS
TILACOIDES
Triticum - enzymology
Triticum - growth & development
TRITICUM AESTIVUM
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Summary:Studies were conducted to identify a 64-kD thylakoid membrane protein of unknown function. The protein was extracted from chloroplast thylakoids under low ionic strength conditions and purified to homogeneity by preparative sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Four peptides generated from the proteolytic cleavage of the wheat 64-kD protein were sequenced and found to be identical to internal sequences of the chloroplast-coupling factor (CF1) alpha-subunit. Antibodies for the 64-kD protein also recognized the alpha-subunit of CF1. Both the 64-kD protein and the 61-kD CF1 alpha-subunit were present in the monocots barley (Hordeum vulgare), maize (Zea mays), oat (Avena sativa), and wheat (Triticum aestivum); but the dicots pea (Pisum sativum), soybean (Glycine max Merr.), and spinach (Spinacia oleracea) contained only a single polypeptide corresponding to the CF1 alpha-subunit. The 64-kD protein accumulated in response to high irradiance (1000 micromol photons m-2 s-1) and declined in response to low irradiance (80 micromol photons m-2 s-1) treatments. Thus, the 64-kD protein was identified as an irradiance-dependent isoform of the CF1 alpha-subunit found only in monocots. Analysis of purified CF1 complexes showed that the 64-kD protein represented up to 15% of the total CF1 alpha-subunit
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.116.2.703