Cloning and Sequence Analysis of the Structural Gene for the bc 1 - Type Rieske Iron-Sulfur Protein from Thermus thermophilus HB8
dc.contributor.author | Gatti, Domenico L. | en_US |
dc.contributor.author | Tarr, George E. | en_US |
dc.contributor.author | Fee, James A. | en_US |
dc.contributor.author | Ackerman, Sharon H. | en_US |
dc.date.accessioned | 2006-09-11T15:17:30Z | |
dc.date.available | 2006-09-11T15:17:30Z | |
dc.date.issued | 1998-06 | en_US |
dc.identifier.citation | Gatti, Domenico L.; Tarr, George; Fee, James A.; Ackerman, Sharon H.; (1998). "Cloning and Sequence Analysis of the Structural Gene for the bc 1 - Type Rieske Iron-Sulfur Protein from Thermus thermophilus HB8." Journal of Bioenergetics and Biomembranes 30(3): 223-233. <http://hdl.handle.net/2027.42/44801> | en_US |
dc.identifier.issn | 0145-479X | en_US |
dc.identifier.issn | 1573-6881 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44801 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9733089&dopt=citation | en_US |
dc.description.abstract | The structural gene encoding the Rieske iron-sulfur protein from Thermus thermophilus HB8 has been cloned and sequenced. The gene encodes a protein of 209 amino acids that begins with a hydrophilic N-terminus followed by a stretch of 21 hydrophobic amino acids that could serve as a transmembrane helix. The remainder of the protein has a hydrophobicity pattern typical of a water-soluble protein. A phylogenetic analysis of 26 Rieske proteins that are part of bc 1 or b 6 f complexes shows that they fall into three major groups: eubacterial and mitochondrial, cyanobacterial and plastid, and five highly divergent outliers, including that of Thermus . Although the overall homology with other Rieske proteins is very low, the C-terminal half of the Thermus protein contains the signature sequence CTHLGC-(13X)-CPCH that most likely provides the ligands of the [2Fe-2S] cluster. It is proposed that this region of the protein represents a small domain that folds independently and that the encoding DNA sequence may have been transferred during evolution to several unrelated genes to provide the cluster attachment site to proteins of different origin. The role of individual residues in this domain of the Thermus protein is discussed vis-a-vis the three-dimensional structure of the bovine protein (Iwata et al ., 1996 Structure 4 , 567–579). | en_US |
dc.format.extent | 1603123 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Animal Biochemistry | en_US |
dc.subject.other | Phylogeny of Rieske Proteins | en_US |
dc.subject.other | Rieske Iron-sulfur Protein | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Organic Chemistry | en_US |
dc.subject.other | Bioorganic Chemistry | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | Thermus Thermophilus | en_US |
dc.title | Cloning and Sequence Analysis of the Structural Gene for the bc 1 - Type Rieske Iron-Sulfur Protein from Thermus thermophilus HB8 | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry and Biophysics Research Division, The University of Michigan Medical School, Ann Arbor, Michigan, 48109; Department of Biology, University of California at San Diego, La Jolla, California, 92093 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry and Biophysics Research Division, The University of Michigan Medical School, Ann Arbor, Michigan, 48109 | en_US |
dc.contributor.affiliationum | Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, 48201; Department of Biological Chemistry and Biophysics Research Division, The University of Michigan Medical School, Ann Arbor, Michigan, 48109 | en_US |
dc.contributor.affiliationother | Department of Surgery and Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, 48201 | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 9733089 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44801/1/10863_2004_Article_409077.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1020540702567 | en_US |
dc.identifier.source | Journal of Bioenergetics and Biomembranes | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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