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Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA.

Publication ,  Journal Article
Guerriero, V; Russo, MA; Olson, NJ; Putkey, JA; Means, AR
Published in: Biochemistry
December 30, 1986

Myosin light chain kinases (MLCK) are the most studied of the calmodulin-activated enzymes; however, minimal sequence information is available for the smooth muscle form of the enzyme. The production of an antibody against the enzyme and the use of expression vectors for constructing cDNA libraries have facilitated the isolation of a cDNA for this kinase. The derived amino sequence was found to contain a region of high homology (54%) to the rabbit skeletal muscle enzyme and also very significant homology (35%) to the catalytic subunit of phosphorylase b kinase and cGMP-dependent protein kinase. All of these homologies were found in the known catalytic domains of these enzyme, thus enabling us to predict the location of the catalytic domain for the chicken gizzard myosin light chain kinase. Within the catalytic domain a consensus sequence for an ATP-binding site was located. Subcloning and expression of different regions of the cDNA defined a 192 base pair fragment coding for the calmodulin-binding domain of MLCK. Both of the cAMP-dependent protein kinase phosphorylation sites were identified by sequence homology. A linear model for MLCK is presented placing the various domains in relative position. Northern blot analysis and S1 protection and mapping experiments have revealed that the mRNA for MLCK is 5.5 kilobases in length, but there also exists a second mRNA of 2.7 kilobases that shares a high degree of homology with about 520 base pairs at the 3' end of the cDNA for MLCK.

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Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

December 30, 1986

Volume

25

Issue

26

Start / End Page

8372 / 8381

Location

United States

Related Subject Headings

  • Sequence Homology, Nucleic Acid
  • Plasmids
  • Myosin-Light-Chain Kinase
  • Muscle, Smooth
  • Gizzard, Avian
  • DNA Restriction Enzymes
  • DNA
  • Cloning, Molecular
  • Chickens
  • Biochemistry & Molecular Biology
 

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Guerriero, V., Russo, M. A., Olson, N. J., Putkey, J. A., & Means, A. R. (1986). Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry, 25(26), 8372–8381. https://doi.org/10.1021/bi00374a007
Guerriero, V., M. A. Russo, N. J. Olson, J. A. Putkey, and A. R. Means. “Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA.Biochemistry 25, no. 26 (December 30, 1986): 8372–81. https://doi.org/10.1021/bi00374a007.
Guerriero V, Russo MA, Olson NJ, Putkey JA, Means AR. Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry. 1986 Dec 30;25(26):8372–81.
Guerriero, V., et al. “Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA.Biochemistry, vol. 25, no. 26, Dec. 1986, pp. 8372–81. Pubmed, doi:10.1021/bi00374a007.
Guerriero V, Russo MA, Olson NJ, Putkey JA, Means AR. Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry. 1986 Dec 30;25(26):8372–8381.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

December 30, 1986

Volume

25

Issue

26

Start / End Page

8372 / 8381

Location

United States

Related Subject Headings

  • Sequence Homology, Nucleic Acid
  • Plasmids
  • Myosin-Light-Chain Kinase
  • Muscle, Smooth
  • Gizzard, Avian
  • DNA Restriction Enzymes
  • DNA
  • Cloning, Molecular
  • Chickens
  • Biochemistry & Molecular Biology