cDNA recombinant plasmid complementary to mRNAs for light chains 1 and 3 of mouse skeletal muscle myosin.

Robert, Benoît; Weydert, A.; Caravatti, M; Minty, Adrian; Cohen, Arlette; P, Daubas; Gros, François; Buckingham, M

doi:10.1073/pnas.79.8.2437

Cited by 26 publications

(12 citation statements)

References 36 publications

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“…The mRNAs for both a and e subunits therefore contain long non-coding sequences. Such a large discrepancy between the respective sizes of a protein and its mRNA has been observed previously (Minty et al, 1981;Robert et al, 1982); it is unlikely that the large size of the mRNA is a result of aggregation since formamide gradients were employed and a single peak was observed. In any event, this size difference allows a first separation between a and Py mRNAs.…”

supporting

confidence: 54%

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

et al. 1983

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Using the rabbit reticulocyte cell-free translation system we have estimated during ontogenesis the proportions of in vitro translatable a and oy brain enolase mRNAs, which are two minor mRNA species. No polypeptide precursor to these enzyme subunits appears to be synthesized during translation in vitro. During brain development, the changes in translatable a and 'y mRNA content seem to parallel those of the corresponding antigens. The proportion of each of the enolase mRNAs is highest in adult mouse brain. Mechanisms controlling a and -y antigen expression are discussed. In order to prepare the specific cDNA probes, purification of a and -y mRNAs was undertaken.

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supporting

confidence: 54%

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

et al. 1983

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“…Without nerve, the breast muscle shows an increased synthesis of myosin fast light-chain 1 and a decreased synthesis of fast light-chain 3. There is evidence that fast light-chains 1 and 3 may be coded by the same gene but that variable gene transcript processing results in either one or the other light chain (32,33). A decreased fast light-chain 3 population or an increased ratio of fast light-chain 1/fast light-chain 3 is known to be associated with early stages of breast muscle development (34).…”

Section: Resultsmentioning

confidence: 99%

Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.

Matsuda¹,

Spector²,

Strohman³

1984

Proc. Natl. Acad. Sci. U.S.A.

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Synthesis patterns of myosin heavy-and light-chain isoforms, tropomyosin and troponin, have been studied in chicken fast muscle denervated at both neonatal and adult stages. Denervated neonatal muscle does not synthesize the adult myosin heavy-chain isoform at the time of denervation, but it does synthesize the adult isoform several months after denervation. Thus, innervation does not appear to be necessary for the normal sequential replacement of embryonic and neonatal myosin heavy chain by the adult variant. Nerve is required, however, for the regulation of tropomyosin and troponin expression. Normally the pectoralis major muscle represses synthesis of both (3-tropomyosin and leg-type troponin T during late embryonic development. After denervation, however, the muscle relaxes its ongoing repression of these proteins and significant amounts of both .8-tropomyosin and leg-type troponin T are synthesized by the muscle. Denervation also results in an altered pattern of myosin light-chain synthesis so that the ratio of fast light-chain 3/fast light-chain 1 decreases. Similar results are found in muscle denervated at the adult stage. In denervated muscle, therefore, synthesis of these myofibrillar proteins is not coordinated: ongoing isoform shifts proceed to express an adult pattern of myosin heavy chain while tropomyosin, troponin, and myosin light-chain patterns appear to revert to embryonic configurations.

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“…One cDNA clone, called clone LK466 (a generous gift from Drs P. Grinning and Wade), contains the coding sequence for the entire human ventricular LC1 (Klotz et al, 1982;Hailstones & Grinning, 1990). The other cDNA clone, called clone pGLC450 (a generous gift from Drs M. Buckingham and B. Robert), contains a genomic DNA fragment of a mouse pseudogene encoding one fragment of mouse skeletal muscle light chains, LC1F and LC3 F (Robert et al, 1982(Robert et al, , 1984.…”

Section: Cdna Clones For Construction Of Expression Plasmids and Prodmentioning

confidence: 99%

Probing myosin light chain 1 structure with monoclonal antibodies

Cornillon¹,

Cathiard²,

Eldin³

et al. 1992

J Muscle Res Cell Motil

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Five monoclonal antibodies that react with different regions of myosin light chain 1 from human ventricular myocardial muscle were used to obtain information on interactions between the light chain 1 and heavy chains and generally on the tertiary structure of the light chain 1 within the myosin head. We performed Western blot assays of the five antibodies with myosins from different cardiac and skeletal muscles, with different proteolytic fragments of bovine ventricular myosin light chain 1 (LC1) and to different recombinant fragments of human ventricular LC1 and rat fast skeletal light chain LC1/LC3. The five antibodies were mapped in three different regions of the light chain 1: two antibodies mapped within the first eight amino-terminal residues, two between residues 71 and 74, and one between residues 129 and 134. The apparent dissociation constants of the last three antibodies, determined by antibody-antigen equilibria in solution, were lower than when isolated light chains were used as antigens. It is probable that the corresponding amino acids involved in the antibody epitopes were either involved in interactions between the light and heavy myosin subunits, or somehow hindered by the myosin heavy chain bulk. In contrast, the apparent dissociation constants measured for both other antibodies were higher when myosin, rather than isolated light chains, was used as antigen. Thus LC1 fixation to heavy chains within the myosin molecule induced conformation changes at the amino-terminal end of the light chain 1. No difference in the accessibility of this mobile LC1 segment was detected in the presence of actin. Finally, observed differences in epitope accessibility on the light chain LC1 in myosin, as compared with chymotryptic subfragment 1 (SF1), indicated conformational differences between native myosin and extensively studied SF1 molecules.

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cDNA recombinant plasmid complementary to mRNAs for light chains 1 and 3 of mouse skeletal muscle myosin.

Cited by 26 publications

References 36 publications

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.

Probing myosin light chain 1 structure with monoclonal antibodies

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