Low-Molecular-Mass Polypeptide Components of a Photosystem II Preparation from the Thermophilic Cyanobacterium Thermosynechococcus vulcanus
| Autor: | Himadri B. Pakrasi, Hirokazu Egashira, Kazuhiko Satoh, Masahiko Ikeuchi, Maki Yoshio, Hiroyuki Koike, Yasuhiro Kashino |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Cyanobacteria
Photosystem II Physiology Protein subunit Molecular Sequence Data Photosynthetic Reaction Center Complex Proteins macromolecular substances Plant Science Biology Thylakoids Bacterial Proteins Amino Acid Sequence Cloning Molecular Photosynthesis Peptide sequence Sequence Homology Amino Acid Molecular mass Cytochrome b Thermophile Temperature Photosystem II Protein Complex food and beverages Cell Biology General Medicine Cytochrome b Group biology.organism_classification Molecular Weight Biochemistry Green algae |
| Zdroj: | Plant and Cell Physiology. 43:1366-1373 |
| ISSN: | 1471-9053 0032-0781 |
| DOI: | 10.1093/pcp/pcf168 |
| Popis: | Using a recently introduced electrophoresis system [Kashino et al. (2001) Electrophoresis 22: 1004], components of low-molecular-mass polypeptides were analyzed in detail in photosystem II (PSII) complexes isolated from athermophilic cyanobacterium, Thermosynechococcus vulcanus (formerly, Synechococcus vulcanus). PsbE, the large subunit polypeptide of cytochrome b 5 5 9 , showed an apparent molecular mass much lower than the expected one. The unusually large mobility could be attributed to the large intrinsic net electronic charge. All other Coomassie-stained polypeptides were identified by N-terminal sequencing. In addition to the well-known cyanobacterial PSII polypeptides, such as PsbE, F, H, I, L, M, U, V and X, the presence of PsbY, PsbZ and Psb27 was also confirmed in the isolated PSII complexes. Furthermore, the whole amino acid sequence was determined for the polypeptide which was known as PsbN. The whole amino acid sequence revealed that this polypeptide was identical to PsbTc which has been found in higher plants and green algae. These results strongly suggest that PsbN is not a member of the PSII complex. It is also shown that cyanobacteria have cytochrome b 5 5 9 in the high potential form as in higher plants. |
| Databáze: | OpenAIRE |
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