Open AccessAn unusually long non-coding region in rat lens α-crystallin messenger RNA
Author(s) -
Rob J.M. Moorman,
Huub M.W. van der Velden,
H. Dodemont,
P. M. Andreoli,
H. Bloemendal,
John G.G. Schoenmakers
Publication year - 1981
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/9.19.4813
Subject(s) - biology , messenger rna , coding region , complementary dna , translational frameshift , rna , untranslated region , nucleic acid sequence , microbiology and biotechnology , nucleotide , dna , peptide sequence , crystallin , base pair , genetics , translation (biology) , gene
Most of the mRNA sequence coding for the alpha A2 chain of the ocular lens protein alpha-crystallin from rat, has been determined by sequencing cloned DNA copies of this mRNA. The 892-base pair cDNA sequence encompasses all but 52 N-terminal amino acids of the alpha A2 chain. It lacks the sequence characteristic for the 22 extra amino acids inserted in the alpha A2 -like chain, named alpha AIns. A stretch of 583 nuceotides, representing more than 50% of the entire mRNA sequence, is located 3' wards of the alpha A2 coding sequence. It contains the characteristic AAUAAA signal involved in poly(A) -addition and represents an unexpectedly long non-coding region. Examination of the total cytoplasmic poly(A) RNA of rat lens by filter-hybridization and subsequent translation of the electrophoretically separated mRNA fractions shows that the alpha A2 chain is encoded by mRNA species which are distinct from the alpha AIns encoding mRNA. No evidence is obtained for an extensive size heterogeneity in the 3' untranslated regions of these two different rat lens mRNAs.
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