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B6db references: 90344765

type Journal Article
authors Bousquet-Lemercier, B.; Pol, S.; Pave-Preux, M.; Hanoune, J.; Barouki, R.
title Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection
journal Biochemistry
ui 90344765
year (1990)
volume 29
number 22
pages 5293-9.
keywords Amino Acid Sequence
abstract Human cytosolic aspartate aminotransferase (cAspAT) cDNA clones have been isolated from an adult human liver cDNA library. Among the clones, two cDNAs of 1550 and 1950 base pairs, respectively, have been characterized. These two cDNAs differ only in the lengths of their 3' noncoding regions and by the presence of one or two putative polyadenylation signals AATAAA. Northern blot analysis revealed two different mRNAs of 2.1 and 1.8 kbp in several human tissues, whereas Southern blot analysis suggested the existence of a single gene for the human cAspAT. The two mRNA species result from the alternative use of two polyadenylation signals. In the liver, the relative ratio of these mRNAs varies among different species and, in humans at least, during development. The properties of the two mRNAs were compared. The half- lives of the 2.1 and 1.8 kbp mRNAs, in the HepG2 cell line, are 8 and 12 h, respectively. The two mRNAs have similar and rather short poly(A) tracts of 20-50 nucleotides. Both mRNAs are capable of directing the in vitro synthesis of the cAspAT protein. We conclude that both the 2.1 and 1.8 kbp cAspAT mRNAs are functional and exhibit similar properties.
last changed 2002/11/04 17:41

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