Abstract
We describe two related manganese-binding polypeptides with L-arginine metabolizing enzyme activity that can be detected as distinct components (designated PsbY-A1 and PsbY-A2, previously called L-AME) in membranes containing Photosystem II (PS II) from spinach. The polypeptides are bitopic and appear to exist in a heterodimeric form, but only in the chlorophyll a/b lineage of plants. Both proteins are encoded in the nucleus. In spinach and in Arabidopsis thaliana they are both derived from a single-copy gene (psbY) that is translated into a precursor polyprotein of approximately 20 kDa. The processing of the polyprotein is complex and includes at least four cleavage steps. Both polypeptides are exposed N-terminally to the lumenal and C-terminally to the stromal face of the thylakoid membrane.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arabidopsis / genetics
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Arabidopsis Proteins*
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Arginine / metabolism
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Base Sequence
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Biological Transport
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Brassicaceae / genetics*
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Cell Compartmentation
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Cell Nucleus / genetics
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DNA, Complementary / genetics
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Dimerization
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Evolution, Molecular
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Gene Dosage
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Gene Library
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Manganese / metabolism*
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Membrane Proteins / genetics*
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Plant Proteins*
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Protein Precursors / metabolism
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Protein Processing, Post-Translational
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Sequence Analysis
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Sequence Homology, Amino Acid
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Spinacia oleracea / genetics
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Ureohydrolases / genetics*
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Ureohydrolases / isolation & purification
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Ureohydrolases / metabolism
Substances
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Arabidopsis Proteins
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DNA, Complementary
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Membrane Proteins
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Plant Proteins
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Protein Precursors
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Manganese
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Arginine
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PSBY protein, Arabidopsis
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PsbY protein, Spinacia oleracea
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Ureohydrolases
Associated data
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GENBANK/AF060198
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GENBANK/AF079800