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Tubulin tyrosine ligase: Protein and mRNA expression in developing rat skeletal muscle
Author(s) -
Arregui Carlos O.,
Mas Carlos R.,
Argaraña Carlos E.,
Barra Héctor S.
Publication year - 1997
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1046/j.1440-169x.1997.t01-1-00005.x
Subject(s) - myogenesis , dna ligase , ubiquitin ligase , biology , microbiology and biotechnology , messenger rna , skeletal muscle , complementary dna , myocyte , biochemistry , ubiquitin , enzyme , endocrinology , gene
Alpha tubulin can be post‐translationally tyrosinated at the carboxy‐terminus by a specific enzyme: tubulin tyrosine ligase. The expression of tubulin tyrosine ligase mRNA and protein during the development of rat skeletal muscle was examined in the present study. A portion of the coding region of the rat ligase cDNA was isolated and sequenced. The nucleotide and amino acid sequences showed about 90% homology with previously reported porcine and bovine ligase sequences. In newborn rats, ligase mRNA and protein were highly expressed in skeletal muscle. During early postnatal development, however, both ligase mRNA and protein dropped down dramatically. Quantitative measurements revealed that ligase protein at postnatal day 20 represented only 10% or less of the level at postnatal day 1. Ligase mRNA expression was also examined during the myogenesis in vitro . A strong ligase mRNA signal was detected in both undifferentiated myoblasts and cross‐striated, contractile myotubes. The present results suggest that, during muscle differentiation, ligase function may be regulated by the amount of available mRNA. The discrepancy in the ligase expression between the in vivo and in vitro myogenesis suggests that factors controlling the levels of mRNA in vivo are lost in vitro .