Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M204137200 on July 2, 2002

J. Biol. Chem., Vol. 277, Issue 37, 34271-34279, September 13, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/37/34271    most recent
M204137200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Patel-King, R. S.
Right arrow Articles by King, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Patel-King, R. S.
Right arrow Articles by King, S. M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

A Bipartite Ca2+-regulated Nucleoside-diphosphate Kinase System within the Chlamydomonas Flagellum
THE REGULATORY SUBUNIT p72*

Ramila S. Patel-King, Sharon E. Benashski, and Stephen M. KingDagger

From the Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030-3305

Regulation of flagellar activity in Chlamydomonas involves both Ca2+ and cAMP-mediated signaling pathways. However, Chlamydomonas and sea urchin sperm flagella also exhibit nucleoside-diphosphate kinase (NDK) activity, suggesting a requirement for GTP within this highly conserved organelle. In sea urchin sperm, the NDK catalytic subunit is an integral component of the outer dynein arm. Here we describe a modular protein (p72) from the Chlamydomonas flagellum that consists of three domains closely related to the presumptive regulatory segment of rat NDK-7 followed by two EF-hands that are predicted to bind Ca2+. There are close homologues of p72 in both mammalian and insect genomes. The p72 protein is tightly associated with the flagellar axoneme and is located along the entire length except at the transition zone. Cross-linking experiments suggest that p72 interacts with two or three additional axonemal polypeptides. The sensitivity of p72 to tryptic digestion differed considerably in the presence and the absence of Ca2+, suggesting that it indeed binds this ligand. These studies indicate that the flagellar NDK system is bipartite with the regulatory and catalytic components residing on different polypeptides. We propose that Ca2+ regulation of flagellar motility in Chlamydomonas may be achieved in part through a downstream GTP-mediated signaling pathway.


* This work was supported by Grant GM51293 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) BK000460.

Dagger Investigator of the Patrick and Catherine Weldon Donaghue Medical Research Foundation. To whom correspondence should be addressed: Dept. of Biochemistry, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030-3305. Tel.: 860-679-3347; Fax: 860-679-3408; Email: steve@king2.uchc.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
B. Duriez, P. Duquesnoy, E. Escudier, A.-M. Bridoux, D. Escalier, I. Rayet, E. Marcos, A.-M. Vojtek, J.-F. Bercher, and S. Amselem
A common variant in combination with a nonsense mutation in a member of the thioredoxin family causes primary ciliary dyskinesia
PNAS, February 27, 2007; 104(9): 3336 - 3341.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Kinukawa, M. Nomura, and V. D. Vacquier
A Sea Urchin Sperm Flagellar Adenylate Kinase with Triplicated Catalytic Domains
J. Biol. Chem., February 2, 2007; 282(5): 2947 - 2955.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
D. M. Baron, K. S. Ralston, Z. P. Kabututu, and K. L. Hill
Functional genomics in Trypanosoma brucei identifies evolutionarily conserved components of motile flagella
J. Cell Sci., February 1, 2007; 120(3): 478 - 491.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
N. Okita, N. Isogai, M. Hirono, R. Kamiya, and K. Yoshimura
Phototactic activity in Chlamydomonas 'non-phototactic' mutants deficient in Ca2+-dependent control of flagellar dominance or in inner-arm dynein
J. Cell Sci., February 1, 2005; 118(3): 529 - 537.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
R. S. Patel-King, O. Gorbatyuk, S. Takebe, and S. M. King
Flagellar Radial Spokes Contain a Ca2+-stimulated Nucleoside Diphosphate Kinase
Mol. Biol. Cell, August 1, 2004; 15(8): 3891 - 3902.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
T. J. Pullen, M. L. Ginger, S. J. Gaskell, and K. Gull
Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum
Mol. Biol. Cell, July 1, 2004; 15(7): 3257 - 3265.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
M. J. Wargo, M. A. McPeek, and E. F. Smith
Analysis of microtubule sliding patterns in Chlamydomonas flagellar axonemes reveals dynein activity on specific doublet microtubules
J. Cell Sci., May 15, 2004; 117(12): 2533 - 2544.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. M. Sadek, A. Jimenez, A. E. Damdimopoulos, T. Kieselbach, M. Nord, J.-A. Gustafsson, G. Spyrou, E. C. Davis, R. Oko, F. A. van der Hoorn, et al.
Characterization of Human Thioredoxin-like 2. A NOVEL MICROTUBULE-BINDING THIOREDOXIN EXPRESSED PREDOMINANTLY IN THE CILIA OF LUNG AIRWAY EPITHELIUM AND SPERMATID MANCHETTE AND AXONEME
J. Biol. Chem., April 4, 2003; 278(15): 13133 - 13142.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Ikeda, J. A. Brown, T. Yagi, J. M. Norrander, M. Hirono, E. Eccleston, R. Kamiya, and R. W. Linck
Rib72, a Conserved Protein Associated with the Ribbon Compartment of Flagellar A-microtubules and Potentially Involved in the Linkage between Outer Doublet Microtubules
J. Biol. Chem., February 21, 2003; 278(9): 7725 - 7734.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement