Sequence analysis of theChlamydomonas reinhardtii flagellar α dynein gene

✍ Scribed by Mitchell, David R. ;Brown, Kimberly S.

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 277 KB
• Volume: 37
• Category: Article
• ISSN: 0886-1544
• DOI: 10.1002/(sici)1097-0169(1997)37:2<120::aid-cm4>3.0.co;2-c

✦ Synopsis

Flagellar outer row dynein ATPases have been used extensively as model systems for studies of microtubule-based motility. Previously full-length sequences were only available for two of the three catalytic heavy-chain subunits (DHCs) of this enzyme. We have completed the sequence of an 18-kb genomic region encoding the Chlamydomonas reinhardtii flagellar outer row dynein a heavy chain. Unlike the band g-subunits, DHC a is not required for assembly of other outer row dynein proteins, except for a tightly associated light chain, and thus occupies a unique position within this enzyme complex. The predicted 4,499 residue protein retains sequence homology to other dynein heavy chains throughout its central and C-terminal regions but lacks homology to any other dyneins in the first 1,000 amino acids, which may account for its unusual assembly properties. This N-terminal domain of DHC a contains a repetitive sequence rich in alanines, prolines, and glutamic acids. Within the more homologous C-terminal region, which includes the catalytic domain, three short sequences unique to DHC a may account for its specific catalytic properties and in vivo phosphorylation pattern.