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J Biol Chem, Vol. 274, Issue 43, 30826-30831, October 22, 1999
From the Department of Pharmacology, Baylor College of Medicine,
One Baylor Plaza, Houston, Texas 77030
A fraction of the signal recognition particle
(SRP) RNA from human, rat, Xenopus, and Saccharomyces
cerevisiae cells contains a single post-transcriptionally added
adenylic acid residue on its 3'-end; in the case of human SRP RNA, over
60% of the SRP RNA molecules contain a nontemplated adenylic acid
residue on their 3'-ends (Sinha, K. M., Gu, J., Chen, Y., and
Reddy, R. (1998) J. Biol. Chem. 273, 6853-6859). In
this study, we investigated the enzyme that is involved in this 3'-end
adenylation of SRP RNA. A U1A protein peptide conjugated to albumin
completely inhibited the polyadenylation of a SV40 mRNA by HeLa
cell nuclear extract in vitro; however, the 3'-end
adenylation of human SRP RNA or Alu RNA, which corresponds
to 5' and 3'-ends of SRP RNA, was not affected by this U1A peptide
conjugate. SRP RNA from mutant strains of S. cerevisiae
with a temperature-sensitive mRNA poly(A) polymerase grown at a
restrictive temperature of 37 °C also contained a
post-transcriptionally added adenylic acid residue just like SRP RNA
from wild-type cells and mutant cells grown at permissive temperature
of 23 °C. In addition, binding of SRP 9/14-kDa protein heterodimer
was required for adenylation of Alu RNA in
vitro. These lines of evidence, along with other data, show that
post-transcriptional adenylation of SRP and Alu RNAs is
carried out by a novel enzyme that is distinct from the mRNA
poly(A) polymerase, CCA-adding enzyme, and nonspecific terminal transferase.
Post-transcriptional Adenylation of Signal Recognition
Particle RNA Is Carried Out by an Enzyme Different from mRNA
Poly(A) Polymerase
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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