Identification of photosystem I components from the cyanobacterium, <i>Synechococcus vulcanus</i> by N‐terminal sequencing
FEBS LettersPublished 14 August 1989Open access
Hiroyuki Koike, Masahiko Ikeuchi, Tetsuo Hiyama, Yorinao Inoue
Citations61
SJR quartileQ1
SJR score1.22
SNIP0.77
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TL;DR
The photosystem I core complex isolated from a thermophilic cyanobacterium, Synechococcus vulcanus, is composed of eight low‐molecular‐mass proteins of 18, 14, 12, 9.5, 9, 6.5 and 4.1 kDa in addition to the PS I chlorophyll protein, which shows appreciable homology with respective subunits of higher plant PS I.
Abstract
The photosystem I core complex isolated from a thermophilic cyanobacterium, Synechococcus vulcanus, is composed of eight low-molecular-mass proteins of 18, 14, 12, 9.5, 9, 6.5, 5 and 4.1 kDa in addition to the PS I chlorophyll protein. N-terminal amino acid sequences of all these components were determined and compared with those of higher plants. Clearly, the 9.5 kDa component corresponds to the protein which carries the non-heme iron-sulfur centers A and B. This protein is so poorly visualized by staining that it has probably been overlooked in gel electrophoresis analyses. The 18, 14, 12 and 9 kDa components show appreciable homology with respective subunits of higher plant PS I. In contrast, the 6.5, 5 and 4.1 kDa components do not correspond to any known proteins except that the sequence of the 4.1 kDa component matches an unidentified open reading frame (ORF) 42 (liverwort) or ORF44 (tobacco) of chloroplast DNA.
Keywords
Biochemistry, Genetics and Molecular Biology
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