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Identification of photosystem I components from the cyanobacterium, Synechococcus vulcanus by N‐terminal sequencing
Author(s) -
Koike Hiroyuki,
Ikeuchi Masahiko,
Hiyama Tetsuo,
Inoue Yorinao
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80971-8
Subject(s) - synechococcus , photosystem ii , biochemistry , molecular mass , open reading frame , chloroplast , biology , photosystem i , cyanobacteria , gel electrophoresis , homology (biology) , peptide sequence , amino acid , chemistry , microbiology and biotechnology , photosynthesis , enzyme , gene , genetics , bacteria
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.