Cloning and characterization of a vertebrate cellular myosin regulatory light chain complementary DNA. 1990

P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
Department of Biotechnology-Molecular Biology, Schering-Plough Corporation, Bloomfield, NJ 07003.

We have isolated two series of complementary DNAs (cDNAs) from a chicken gizzard cDNA library encoding two isoforms of phosphorylatable myosin regulatory light chain (RLC). One of the cDNAs encodes a previously isolated smooth muscle myosin RLC (also referred to as LC20-A); the other encodes a protein that shares 92% homology with the LC20-A isoform. The phosphorylatable threonine and serine residues at positions 18 and 19 of the two myosin RLC sequences are conserved. The two cDNAs are 81% homologous at the nucleotide level over the coding region; the 5' and 3' untranslated regions are divergent. Most of the DNA nonhomology in the coding region does not affect the protein sequence, indicating strong evolutionary conservation pressure to maintain the myosin RLC structure. Northern blot analysis using 3' untranslated region probes reveals restrictive tissue specific expression of one myosin RLC isoform (LC20-A) in smooth muscle tissue and not in other tissues examined. In contrast, the novel myosin RLC isoform messenger RNA (mRNA) is uniformly expressed in all smooth and nonmuscle tissues examined and is designated as cellular myosin RLC for this reason. Our results indicate that cellular and smooth muscle myosin RLC isoforms are distinct and are encoded by separate genes. This report describes the cloning of a novel vertebrate cellular myosin RLC mRNA that differs from previously characterized smooth muscle RLC isoform mRNAs in both primary sequence and expression pattern.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009219 Myosin-Light-Chain Kinase An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction. Myosin Kinase,Myosin LCK,Myosin Regulatory Light-Chain Kinase,Kinase, Myosin,Kinase, Myosin-Light-Chain,LCK, Myosin,Myosin Light Chain Kinase,Myosin Regulatory Light Chain Kinase
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004095 Dihydropyridines Pyridine moieties which are partially saturated by the addition of two hydrogen atoms in any position.
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005895 Gizzard, Avian The posterior portion of the avian stomach located between the PROVENTRICULUS and INTESTINE. It consists of a thick muscular wall and small stones (gastroliths) that function to mechanically grind SEEDS and other ingested objects. Gizzard,Ventriculus,Avian Gizzard,Avian Gizzards,Gizzards,Gizzards, Avian
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
August 1987, The Journal of biological chemistry,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
October 1989, Proceedings of the National Academy of Sciences of the United States of America,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
October 2008, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
August 2005, Parasitology research,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
November 1993, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
July 1988, FEBS letters,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
February 2009, Circulation journal : official journal of the Japanese Circulation Society,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
December 2015, Cytoskeleton (Hoboken, N.J.),
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
October 1997, Journal of molecular and cellular cardiology,
P J Zavodny, and M E Petro, and H K Lonial, and S H Dailey, and S K Narula, and P J Leibowitz, and C C Kumar
April 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire,
Copied contents to your clipboard!