Nucleic Acids Research, 1993, Vol. 21, No. 7 1555-1562
© 1993
MOLECULAR BIOLOGY |
The biochemical defects of prp4-1 and prp6-1 yeast splicing mutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP
Unité de Génétique Moléculaire des Levures, Département de Biologie Moléculaire, Institut Pasteur 28 rue du Docteur Roux, Paris 75724, France
* To whom correspondence should be addressed
Received January 26, 1993. Accepted February 26, 1993.
We have raised specific antibodies against the PRP6 protein and shown that the U4, U5 and U6 snRNAs are co-precipitated with this protein. Using splicing extracts prepared from In vivo heat-inactivated cells, we have characterized the prp4–1 and prp6–1 biochemical defects. In inactivated prp4-1 cell extracts, the U6 snRNA content as well as the U6, U4/U6 snRNPs and the [U4/U6.U5] tri-snRNP particles amounts are severely reduced. In inactivated prp6–1 cell extracts, the PRP6 mutant protein is barely detectable. Glycerol gradient analyses indicate that, in these extracts, the [U4/U6.U5] tri-snRNPs are present in very low amounts, but U4/U6 snRNP particles are normally represented. These results establish that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP. We found no evidence for the presence of the PRP6 protein in the U4/U6 particle.
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