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Nucleic Acids Research, 1988, Vol. 16, No. 9 3751-3770
© 1988


Articles

cDNA cloning of human hnRNP protein Al reveals the existence of multiple mRNA isoforms

M. Buvoli, G. Biamonti, P. Tsoulfas, M.T. Bassi, A. Ghetti, S. Riva* and C. Morandi1

Istituto di Genetica Biochimica ed Evoluzionistica, CNR, Via Abbiategrasso 207-27100 Pavia 1Istituto di Scienze Biologiche, Università degli Studi di Verona Italy

*To whom correspondence should be addressed

Received February 2, 1988. Revised March 24, 1988. Accepted March 24, 1988.

Protein Al is one of the major component of mammalian ribonucleoprotein particles (hnRNP). Human protein Al cDNA cloning and sequencing revealed the existence of at least two protein isoforms. Among the cDNAs examined, sequence differences were found both in the structural portion, leading to aminoacid changes (Tyr to Phe or Arg to Lys) and in the non +ranslated 3'-region where two T-stretches of different length were observed. Interestingly one of the aminoacid substitutions falls into a consensus sequence common to many RNA binding proteins. Northern blot analysis of poly A+ RNAs from five human tissues revealed two mRNA forms of 1500 and 1900 n due to alternative polyadenylation. Analysis of genomic DNA showed at least 30 A1-specific sequences, some of which correspond to processed pseudogenes. These results suggest that protein Al is encoded by a multigene family.


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