Nucleic Acids Research, Vol 24, Issue 13 2535-2542, Copyright © 1996 by Oxford University Press
R Gattoni, D Mahe, P Mahl, N Fischer, MG Mattei, J Stevenin and JP Fuchs
With anti-hnRNP monoclonal antibody 6D12 we previously showed in HeLa cells
that as early as 10 min after the onset of a heat shock at 45 degrees C, a
72.5-74 kDa antigen doublet leaves the hnRNPs and strongly associates with
the nuclear matrix, the effect being reversed after a 6 h recovery at 37
degrees C. cDNA cloning and sequencing enabled us to identify these
antigens as hnRNP-M proteins and further to show that the correct sequence
differs by an 11 amino acid stretch from the originally published sequence.
We also show that monoclonal antibodies raised against synthetic hnRNP-M
peptides can directly inhibit in vitro splicing. Furthermore, stressing
cells at 45 degrees C for 10 min is sufficient to abolish the splicing
capacity of subsequently prepared nuclear extracts which, interestingly, do
not contain the hnRNP-M proteins any more. Taken together, our data suggest
that these proteins are involved in splicing as well as in early
stress-induced splicing arrest. Further in situ hybridization assays
located the hnRNP-M encoding gene on human chromosome 19.
ARTICLES
The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping
Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/ULP, C.U. De Strasbourg, France.
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