Purification of calmodulin from Chlamydomonas: calmodulin occurs in cell bodies and flagella

doi:10.1083/jcb.87.3.764

This Article

	Full Text (PDF, 1235K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Gitelman, S. E.
	Articles by Witman, G. B.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Gitelman, S. E.
	Articles by Witman, G. B.


Social Bookmarking

	What's this?

ARTICLES

Purification of calmodulin from Chlamydomonas: calmodulin occurs in cell bodies and flagella

SE Gitelman and GB Witman

Calmodulin has been purified from cell bodies of the green alga Chlamydomonas by Ca++-dependent affinity chromatography on fluphenazine- Sepharose 4B. Calmodulin from this primitive organism closely resembles that from bovine brain in a number of properties, including (a) binding to fluphenazine in a Ca++-dependent, reversible manner, (b) functioning as a heat-stable, Ca++-dependent activator of cyclic nucleotide phosphodiesterase, and (c) electrophoretic mobility in SDS- polyacrylamide gels in both the presence and absence of Ca++, which causes a shift in the relative mobility of calmodulin. Calmodulin has also been identified by the criteria of phosphodiesterase activation and electrophoretic mobility in both the detergent soluble "membrane plus matrix" and the axoneme fractions of Chlamydomonas flagella. Calmodulin is not associated with the partially purified 12S or 18S dynein ATPases of Chlamydomonas. The presence of calmodulin in the flagellum suggests that it is involved in one or more of the Ca++- dependent activities of this organelle.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Dymek, E. E., Goduti, D., Kramer, T., Smith, E. F. (2006). A kinesin-like calmodulin-binding protein in Chlamydomonas: evidence for a role in cell division and flagellar functions. J. Cell Sci. 119: 3107-3116 [Abstract] [Full Text]
Ignotz, G. G., Suarez, S. S. (2005). Calcium/Calmodulin and Calmodulin Kinase II Stimulate Hyperactivation in Demembranated Bovine Sperm. Biol. Reprod. 73: 519-526 [Abstract] [Full Text]
Patel-King, R. S., Gorbatyuk, O., Takebe, S., King, S. M. (2004). Flagellar Radial Spokes Contain a Ca2+-stimulated Nucleoside Diphosphate Kinase. Mol. Biol. Cell 15: 3891-3902 [Abstract] [Full Text]
Casey, D. M., Yagi, T., Kamiya, R., Witman, G. B. (2003). DC3, the Smallest Subunit of the Chlamydomonas Flagellar Outer Dynein Arm-docking Complex, Is a Redox-sensitive Calcium-binding Protein. J. Biol. Chem. 278: 42652-42659 [Abstract] [Full Text]
Patel-King, R. S., Benashski, S. E., King, S. M. (2002). A Bipartite Ca2+-regulated Nucleoside-diphosphate Kinase System within the Chlamydomonas Flagellum. THE REGULATORY SUBUNIT p72. J. Biol. Chem. 277: 34271-34279 [Abstract] [Full Text]
Smith, E. F. (2002). Regulation of Flagellar Dynein by Calcium and a Role for an Axonemal Calmodulin and Calmodulin-dependent Kinase. Mol. Biol. Cell 13: 3303-3313 [Abstract] [Full Text]
Yang, P., Diener, D. R., Rosenbaum, J. L., Sale, W. S. (2001). Localization of Calmodulin and Dynein Light Chain Lc8 in Flagellar Radial Spokes. JCB 153: 1315-1326 [Abstract] [Full Text]
Finst, R., Kim, P., Griffis, E., Quarmby, L. (2000). Fa1p is a 171 kDa protein essential for axonemal microtubule severing in Chlamydomonas. J. Cell Sci. 113: 1963-1971 [Abstract]
Harrison, A., Olds-Clarke, P., King, S. M. (1998). Identification of the t Complex-encoded Cytoplasmic Dynein Light Chain Tctex1 in Inner Arm I1 Supports the Involvement of Flagellar Dyneins in Meiotic Drive. JCB 140: 1137-1147 [Abstract] [Full Text]