The genes and mRNA coding for the heavy chains of chick embryonic skeletal myosin

Patrinou-Georgoulas, Meropi; John, Huw A.

doi:10.1016/0092-8674(77)90125-8

Cited by 18 publications

(3 citation statements)

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“…This system had been optimized for both MHC synthesis and total protein synthesis (2). In both instances the MHC mRNA activity sedimented at approximately 26 S, in good agreement with the previously reported sedimentation value for other MHC mRNAs from other systems (15)(16)(17). MHC represented about 3040% of the total protein synthesis directed by the RNA from two peak gradient fractions.…”

Section: Resultssupporting

confidence: 61%

“…The most abundant class had a calculated complexity of 5980 nucleotides. Because chicken MHC mRNA has been reported to be 6000 nucleotides long (16,17,19,20), it appeared that MHC mRNA was the most abundant RNA in this population.…”

Section: Resultsmentioning

confidence: 99%

“…Recently Patrinou-Georgoulas and John (17) have isolated a MHC mRNA from embryonic chicken muscle with a nucleotide sequence complexity very similar to the rat MHC mRNA reported here.…”

Section: Discussionmentioning

confidence: 99%

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Most myosin heavy chain mRNA in L6E9 rat myotubes has a short poly(A) tail.

Benoff¹,

Nadal‐Ginard²

1979

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

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ABSITRACT The mRNA for rat muscle myosin heavy chain (MHC) was isolated from L6E9 myotubes by two rounds of sucrose density gradient centrifugation followed by fractionation on an agarose/polyacrylamide gel. Cultured rat myogenic cell lines (1) provide an in vitro model system for the study of myogenesis. The biochemical and morphological changes that occur during the differentiation of these cell lines parallels those occurring during myogenesis in viw. Multinucleated fibers are formed by the fusion of single myoblasts. Concomitant with cell fusion, there begins the synthesis and accumulation of muscle-specific contractile proteins, such as the heavy and light chains of myosin, actin, tropomyosin, and the troponins.We were interested in determining whether changes in myosin heavy chain (MHC; Mr = 200,000) accumulation during myogenic differentiation could be correlated with parallel changes in the level of cytoplasmic MHC mRNA. We had previously developed an in vitro translational system (2), which we employed to monitor for the presence of MHC mRNA. However, because it is possible that MHC mRNA can be sequestered in a manner that prevents its translation (3), it is necessary to directly measure the amount of MHC mRNA by hybridization with complementary DNA (cDNA) to pure MHC mRNA.We report here on the isolation and purification of a mammalian MHC mRNA. The cDNA prepared with this mRNA as template has been used to investigate the controls on MHC accumulation during myogenesis. The data indicate that the level of cytoplasmic MHC mRNA increases nt200-fold as the dividing myoblast differentiates into the fused myotube. A striking feature of this increase in MHC mRNA accumulation is its compartmentalization. The largest increase in cytoplasmic MHC mRNA occurs in that RNA population that fails to bind to oligo(dT)-cellulose.

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Section: Resultssupporting

confidence: 61%

Section: Resultsmentioning

confidence: 99%