| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 274, Issue 51, 36213-36218, December 17, 1999
,,¶
From the The calcium/calmodulin-dependent
activation of nitric-oxide synthase (NOS) and its production of nitric
oxide (NO) play a key regulatory role in plant and animal cell
function. SCaM-1 is a plant calmodulin (CaM) isoform that is 91%
identical to mammalian CaM (wild type CaM (wtCaM)) and a selective
competitive antagonist of NOS (Cho, M. J., Vaghy, P. L.,
Kondo, R., Lee, S. H., Davis, J. P., Rehl, R., Heo, W. D., and Johnson, J. D. (1998) Biochemistry 37, 15593-15597). We have used site-directed mutagenesis to show that a
point mutation, involving the substitution of valine for methionine at
position 144, is responsible for SCaM-1's inhibition of mammalian NOS.
An M144V mutation in wild type CaM produced a mutant (M144V) which
exhibited nearly identical inhibition of NOS's NO production and NADPH
oxidation, with a similar Ki (~15 nM)
as SCaM-1. A V144M back mutation in SCaM-1 significantly restored its
ability to activate NOS's catalytic functions. The length of the
hydrophobic amino acid side chain at position 144 appears to be
critical for NOS activation, since M144L and M144F activated NOS while
M144V and M144C did not. Despite their competitive antagonism of NOS,
M144V, like SCaM-1, exhibited a similar dose-dependent activation of phosphodiesterase and calcineurin as wtCaM. SCaM-1 and
M144V produced greater inhibition of NOS's oxygenase domain function
(NO production) than its reductase domain functions (NADPH oxidation
and cytochrome c reduction). Thus, CaM's methionine 144 plays a critical role the activation of NOS, presumably by influencing
the function of NOS's oxygenase domain.
Department of Molecular and Cellular
Biochemistry, The Ohio State University Medical Center, Columbus,
Ohio 43210 and the § Department of Biochemistry, Plant
Molecular Biology and Biotechnology Research Center, Gyeongsang
National University, Chinju 660-701, Korea
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  H. Ishida, H. Huang, A. P. Yamniuk, Y. Takaya, and H. J. Vogel The Solution Structures of Two Soybean Calmodulin Isoforms Provide a Structural Basis for Their Selective Target Activation Properties J. Biol. Chem., May 23, 2008; 283(21): 14619 - 14628. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. S. Sharp and K. B. Tomer Analysis of the Oxidative Damage-Induced Conformational Changes of Apo- and Holocalmodulin by Dose-Dependent Protein Oxidative Surface Mapping Biophys. J., March 1, 2007; 92(5): 1682 - 1692. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Tiso, D. W. Konas, K. Panda, E. D. Garcin, M. Sharma, E. D. Getzoff, and D. J. Stuehr C-terminal Tail Residue Arg1400 Enables NADPH to Regulate Electron Transfer in Neuronal Nitric-oxide Synthase J. Biol. Chem., November 25, 2005; 280(47): 39208 - 39219. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. C. Park, M. L. Kim, Y. H. Kang, J. M. Jeon, J. H. Yoo, M. C. Kim, C. Y. Park, J. C. Jeong, B. C. Moon, J. H. Lee, et al. Pathogen- and NaCl-Induced Expression of the SCaM-4 Promoter Is Mediated in Part by a GT-1 Box That Interacts with a GT-1-Like Transcription Factor Plant Physiology, August 1, 2004; 135(4): 2150 - 2161. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Vougier, J. Mary, N. Dautin, J. Vinh, B. Friguet, and D. Ladant Essential Role of Methionine Residues in Calmodulin Binding to Bordetella pertussis Adenylate Cyclase, as Probed by Selective Oxidation and Repair by the Peptide Methionine Sulfoxide Reductases J. Biol. Chem., July 16, 2004; 279(29): 30210 - 30218. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. P. Yamniuk and H. J. Vogel Structurally Homologous Binding of Plant Calmodulin Isoforms to the Calmodulin-binding Domain of Vacuolar Calcium-ATPase J. Biol. Chem., February 27, 2004; 279(9): 7698 - 7707. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P.-J. Jih, Y.-C. Chen, and S.-T. Jeng Involvement of Hydrogen Peroxide and Nitric Oxide in Expression of the Ipomoelin Gene from Sweet Potato Plant Physiology, May 1, 2003; 132(1): 381 - 389. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Y. Choi, S. H. Lee, C. Y. Park, W. D. Heo, J. C. Kim, M. C. Kim, W. S. Chung, B. C. Moon, Y. H. Cheong, C. Y. Kim, et al. Identification of Calmodulin Isoform-specific Binding Peptides from a Phage-displayed Random 22-mer Peptide Library J. Biol. Chem., June 7, 2002; 277(24): 21630 - 21638. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. C. Kim, S. H. Lee, J. K. Kim, H. J. Chun, M. S. Choi, W. S. Chung, B. C. Moon, C. H. Kang, C. Y. Park, J. H. Yoo, et al. Mlo, a Modulator of Plant Defense and Cell Death, Is a Novel Calmodulin-binding Protein. ISOLATION AND CHARACTERIZATION OF A RICE Mlo HOMOLOGUE J. Biol. Chem., May 24, 2002; 277(22): 19304 - 19314. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. E. Townley and M. R. Knight Calmodulin as a Potential Negative Regulator of Arabidopsis COR Gene Expression Plant Physiology, April 1, 2002; 128(4): 1169 - 1172. [Full Text] [PDF]
|
|
|
|
|
|
S. Adak, J. Santolini, S. Tikunova, Q. Wang, J. D. Johnson, and D. J. Stuehr Neuronal Nitric-oxide Synthase Mutant (Ser-1412 right-arrow Asp) Demonstrates Surprising Connections between Heme Reduction, NO Complex Formation, and Catalysis J. Biol. Chem., January 5, 2001; 276(2): 1244 - 1252. [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 |
