cDNA cloning of the human U1 snRNA-associated A protein: extensive homology between U1 and U2 snRNP-specific proteins.
Open Access
- 1 December 1987
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 6 (12) , 3841-3848
- https://doi.org/10.1002/j.1460-2075.1987.tb02721.x
Abstract
Sera from patients with connective tissue diseases often contain antibodies against snRNA‐associated proteins. Using one of these sera in an immunological screening of a human lambda gt11 expression vector cDNA library, two cDNA clones for the U1 snRNP‐specific A protein, termed lambda HA‐1 and lambda HA‐2, were isolated. Monospecific antibodies, eluted from the beta‐galactosidase fusion protein of either clone reacted with the U1 snRNP‐specific A antigen. The identity of the clones was confirmed by in vitro translation of hybrid selected mRNA. RNA blot analysis revealed a single polyadenylated transcript of about 1.4 kb in human cells. A cDNA of 1.2 kb, isolated from the same lambda gt11 expression library by cross‐hybridization with a lambda HA‐2 restriction fragment, covered the complete coding sequence of the A protein as demonstrated by in vitro translation of an RNA transcript synthesized from this cDNA. The deduced amino acid sequence contains one very hydrophilic region, and internal sequence duplication and a region highly homologous to the RNP consensus sequence that seems to be common to RNA binding proteins. Sequence comparison with the recently cloned U2 snRNP‐specific B′ protein revealed two extremely homologous regions located in the carboxy‐terminal (homology of 86%) and amino‐terminal part (homology of 77%) of the proteins. This structural relationship indicates that proteins A and B′, although located in different snRNP particles, may have identical functions.This publication has 52 references indexed in Scilit:
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