Home LiteratureArticle Details
PMID: 1371510 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Biochemical properties of chimeric skeletal and smooth muscle myosin light chain kinases.

The Journal of biological chemistry ·Vol. 267 ·No. 7 ·1992-03-05 ·Pages 4930-8

Leachman SA, Gallagher PJ, Herring BP, McPhaul MJ, Stull JT

Abstract

The molecular and biochemical properties of myosin light chain kinases from chicken skeletal and smooth muscle were investigated by recombinant DNA techniques. Deletion of the amino-terminal region of either the smooth or skeletal muscle myosin light chain kinase resulted in a decrease in Vmax with no significant change in Km values for light chain substrates. Skeletal/smooth muscle chimeric kinases were inactive when a 65-residue region amino-terminal of the catalytic core was exchanged between the two forms. Changing alanine 494 to glutamic acid within this region in the chicken skeletal muscle myosin light chain kinase increased the Km values for light chains 10-fold. These results are consistent with the hypothesis that the region amino-terminal of the catalytic core in myosin light chain kinases is involved in light chain recognition. A skeletal muscle kinase which contained the smooth muscle calmodulin binding domain remained regulated by Ca2+/calmodulin. Thus, the calmodulin binding domains of smooth and skeletal muscle myosin light chain kinases share structural elements necessary for regulation.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Northern Blotting, Western Calmodulin/metabolism Chickens DNA/genetics DNA, Recombinant/metabolism Kinetics Molecular Sequence Data Muscle, Smooth/enzymology Muscles/enzymology Myosin-Light-Chain Kinase/genetics,metabolism RNA/genetics Recombinant Fusion Proteins/genetics,metabolism Restriction Mapping Sequence Homology, Nucleic Acid Substrate Specificity Transcription, Genetic
Chemicals
Calmodulin DNA, Recombinant Recombinant Fusion Proteins RNA DNA Myosin-Light-Chain Kinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Leachman S A
Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235.
Gallagher P J
Herring B P
McPhaul M J
Stull J T
References (45)
45 references, click to expand
  1. Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase.
    Science. 1988 Aug 19;241(4868):970-3 PMID: 3406746
  2. The structure and organization of the human heavy neurofilament subunit (NF-H) and the gene encoding it.
    EMBO J. 1988 Jul;7(7):1947-55 PMID: 3138108
  3. The expression of a functional cDNA encoding the chicken cytochrome P-450arom (aromatase) that catalyzes the formation of estrogen from androgen.
    J Biol Chem. 1988 Nov 5;263(31):16358-63 PMID: 3182796
  4. Molecular characterization of rat skeletal muscle myosin light chain kinase.
    Am J Physiol. 1989 Feb;256(2 Pt 1):C399-404 PMID: 2465691
  5. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme.
    J Biol Chem. 1989 May 15;264(14):8222-9 PMID: 2722778
  6. Myosin light chain kinase structure function analysis using bacterial expression.
    J Biol Chem. 1989 Sep 25;264(27):15843-9 PMID: 2674119
  7. Domain characterization of rabbit skeletal muscle myosin light chain kinase.
    J Biol Chem. 1990 Jan 25;265(3):1724-30 PMID: 1688558
  8. A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel.
    Anal Biochem. 1989 Nov 15;183(1):139-43 PMID: 2559625
  9. Regulatory and structural motifs of chicken gizzard myosin light chain kinase.
    Proc Natl Acad Sci U S A. 1990 Mar;87(6):2284-8 PMID: 2315320
  10. How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices.
    Trends Biochem Sci. 1990 Feb;15(2):59-64 PMID: 2186516
  11. Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity.
    J Cell Biol. 1990 Sep;111(3):1107-25 PMID: 2202734
  12. Acidic residues comprise part of the myosin light chain-binding site on skeletal muscle myosin light chain kinase.
    J Biol Chem. 1990 Sep 25;265(27):16588-91 PMID: 2398065
  13. Basic residues are important for Ca2+/calmodulin binding and activation but not autoinhibition of rabbit skeletal muscle myosin light chain kinase.
    J Biol Chem. 1991 Jun 25;266(18):11838-41 PMID: 2050680
  14. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
    Science. 1991 Jul 26;253(5018):407-14 PMID: 1862342
  15. Molecular characterization of a mammalian smooth muscle myosin light chain kinase.
    J Biol Chem. 1991 Dec 15;266(35):23936-44 PMID: 1748666
  16. Cleavage at aspartyl-prolyl bonds.
    Methods Enzymol. 1977;47:145-9 PMID: 22018
  17. Purification and characterization of smooth muscle myosin light chain kinase.
    J Biol Chem. 1981 Jul 25;256(14):7501-9 PMID: 6894756
  18. Effects of pH, ionic strength, and temperature on activation by calmodulin an catalytic activity of myosin light chain kinase.
    Biochemistry. 1982 May 11;21(10):2386-91 PMID: 6896461
  19. Shape and substructure of skeletal muscle myosin light chain kinase.
    Biochemistry. 1983 Aug 30;22(18):4316-26 PMID: 6688734
  20. A simple and very efficient method for generating cDNA libraries.
    Gene. 1983 Nov;25(2-3):263-9 PMID: 6198242
  21. Mammalian skeletal muscle myosin light chain kinases. A comparison by antiserum cross-reactivity.
    J Biol Chem. 1984 Feb 10;259(3):1776-80 PMID: 6546381
  22. A comprehensive set of sequence analysis programs for the VAX.
    Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387-95 PMID: 6546423
  23. Selective purification of the 20,000-Da light chains of smooth muscle myosin.
    Anal Biochem. 1983 Nov;135(1):37-43 PMID: 6670746
  24. Oligonucleotide-directed mutagenesis: a simple method using two oligonucleotide primers and a single-stranded DNA template.
    DNA. 1984 Dec;3(6):479-88 PMID: 6096101
  25. Use of o-phthalaldehyde to reduce background during automated Edman degradation.
    Anal Biochem. 1984 Feb;137(1):134-42 PMID: 6428262
  26. Lymphokine purification by reversed-phase high-performance liquid chromatography.
    J Chromatogr. 1984 Jul 27;296:171-9 PMID: 6332819
  27. Myosin light chain phosphorylation in fast and slow skeletal muscles in situ.
    Am J Physiol. 1984 Nov;247(5 Pt 1):C462-71 PMID: 6548609
  28. Rapid and sensitive protein similarity searches.
    Science. 1985 Mar 22;227(4693):1435-41 PMID: 2983426
  29. Functional domains of chicken gizzard myosin light chain kinase.
    J Biol Chem. 1985 Jun 25;260(12):7765-74 PMID: 3838992
  30. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle.
    Annu Rev Pharmacol Toxicol. 1985;25:593-620 PMID: 2988424
  31. Phosphorylation of rabbit skeletal muscle myosin in situ.
    J Cell Physiol. 1985 Nov;125(2):301-5 PMID: 4055914
  32. A rapid and sensitive method for detection and quantification of calcineurin and calmodulin-binding proteins using biotinylated calmodulin.
    Proc Natl Acad Sci U S A. 1985 Nov;82(22):7585-9 PMID: 3865179
  33. Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase.
    Biochemistry. 1985 Oct 22;24(22):6028-37 PMID: 3841288
  34. Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases.
    J Biol Chem. 1986 Jun 25;261(18):8320-6 PMID: 2873140
  35. Amino acid sequence of rabbit skeletal muscle myosin light chain kinase.
    Biochemistry. 1986 Dec 2;25(24):8049-57 PMID: 3542042
  36. The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence.
    J Biol Chem. 1987 Feb 25;262(6):2542-8 PMID: 3818608
  37. Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA.
    Biochemistry. 1986 Dec 30;25(26):8372-81 PMID: 3030394
  38. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
    J Biol Chem. 1987 Jul 25;262(21):10035-8 PMID: 3611052
  39. Protein serine/threonine kinases.
    Annu Rev Biochem. 1987;56:567-613 PMID: 2956925
  40. Sequence analysis of elastin cDNA from chick aorta and tissue-specific transcription of the elastin gene in developing chick embryo.
    Arch Biochem Biophys. 1987 Aug 1;256(2):455-61 PMID: 3502711
  41. Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.
    J Biol Chem. 1987 Sep 5;262(25):11958-63 PMID: 3624242
  42. Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution.
    J Biol Chem. 1988 Jul 25;263(21):10510-6 PMID: 2839493
  43. Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments.
    J Biol Chem. 1987 Oct 5;262(28):13828-34 PMID: 3654638
  44. Myosin light chain kinases and kinetics of myosin phosphorylation in smooth muscle cells.
    Prog Clin Biol Res. 1987;245:183-93 PMID: 3317437
  45. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
    Science. 1988 Jul 1;241(4861):42-52 PMID: 3291115
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1992-03-05
Pages
4930-8
Language
English
Region
United States
NLM ID
2985121R
PMCID
PMC2836765
Subset
IM
Grants
NIGMS NIH HHS · T32 GM008014 · United States
NHLBI NIH HHS · R01 HL026043 · United States
NHLBI NIH HHS · R01 HL026043-20 · United States
NHLBI NIH HHS · R37 HL026043 · United States
NIGMS NIH HHS · 5T-32 GM08014 · United States
NHLBI NIH HHS · HL26043 · United States
Databases
GENBANK
L01674, L01675, L01676, L01677, M81786, M81787, M83326, M83327, M83328, M83368
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com