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Vol. 19, Issue 9, 3724-3734, September 2008
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*Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305; and
Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605
Submitted April 8, 2008;
Revised June 9, 2008;
Accepted June 13, 2008
Monitoring Editor: Erika Holzbaur
The highly conserved LC8/DYNLL family proteins were originally identified in axonemal dyneins and subsequently found to function in multiple enzyme systems. Genomic analysis uncovered a third member (LC10) of this protein class in Chlamydomonas. The LC10 protein is extracted from flagellar axonemes with 0.6 M NaCl and cofractionates with the outer dynein arm in sucrose density gradients. Furthermore, LC10 is specifically missing only from axonemes of those strains that fail to assemble outer dynein arms. Previously, the oda12-1 insertional allele was shown to lack the Tctex2-related dynein light chain LC2. The LC10 gene is located
2 kb from that of LC2 and is also completely missing from this mutant but not from oda12-2, which lacks only the 3' end of the LC2 gene. Although oda12-1 cells assemble outer arms that lack only LC2 and LC10, this strain exhibits a flagellar beat frequency that is consistently less than that observed for strains that fail to assemble the entire outer arm and docking complex (e.g., oda1). These results support a key regulatory role for the intermediate chain/light chain complex that is an integral and highly conserved feature of all oligomeric dynein motors.
These authors contributed equally to this work.
Present address: Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Address correspondence to: Stephen M. King (steve{at}king2.uchc.edu)
Abbreviations used: HC, heavy chain; IC, intermediate chain; LC, light chain; MBP, maltose-binding protein.
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S. M. King Dynein-Independent Functions of DYNLL1/LC8: Redox State Sensing and Transcriptional Control Sci. Signal., November 25, 2008; 1(47): pe51 - pe51. [Abstract] [Full Text] [PDF] |
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