PMID- 10545122
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20201214
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 21
DP  - 1999 Nov 1
TI  - Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5'
      stem-loop of U4 snRNA.
PG  - 6119-33
AB  - Activation of the spliceosome for splicing catalysis requires the dissociation of
      U4 snRNA from the U4/U6 snRNA duplex prior to the first step of splicing. We
      characterize an evolutionarily conserved 15.5 kDa protein of the HeLa [U4/U6.U5] 
      tri-snRNP that binds directly to the 5' stem-loop of U4 snRNA. This protein
      shares a novel RNA recognition motif with several RNP-associated proteins, which 
      is essential, but not sufficient for RNA binding. The 15.5kD protein binding site
      on the U4 snRNA consists of an internal purine-rich loop flanked by the stem of
      the 5' stem-loop and a stem comprising two base pairs. Addition of an RNA
      oligonucleotide comprising the 5' stem-loop of U4 snRNA (U4SL) to an in vitro
      splicing reaction blocked the first step of pre-mRNA splicing. Interestingly,
      spliceosomal C complex formation was inhibited while B complexes accumulated.
      This indicates that the 15.5kD protein, and/or additional U4 snRNP proteins
      associated with it, play an important role in the late stage of spliceosome
      assembly, prior to step I of splicing catalysis. Our finding that the 15.5kD
      protein also efficiently binds to the 5' stem-loop of U4atac snRNA indicates that
      it may be shared by the [U4atac/U6atac.U5] tri-snRNP of the minor U12-type
      spliceosome.
FAU - Nottrott, S
AU  - Nottrott S
AD  - Institut fur Molekularbiologie und Tumorforschung, Philipps-Universitat Marburg, 
      Emil-Mannkopff-Strasse 2, D-35037 Marburg, Germany.
FAU - Hartmuth, K
AU  - Hartmuth K
FAU - Fabrizio, P
AU  - Fabrizio P
FAU - Urlaub, H
AU  - Urlaub H
FAU - Vidovic, I
AU  - Vidovic I
FAU - Ficner, R
AU  - Ficner R
FAU - Luhrmann, R
AU  - Luhrmann R
LA  - eng
SI  - GENBANK/AF155235
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (RNA Precursors)
RN  - 0 (RNA, Small Nuclear)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Ribonucleoproteins, Small Nuclear)
RN  - 0 (Snu13 protein, human)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Binding Sites
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nucleic Acid Conformation
MH  - Phylogeny
MH  - RNA Precursors/genetics
MH  - RNA Splicing
MH  - RNA, Small Nuclear/*metabolism
MH  - RNA-Binding Proteins/chemistry/genetics
MH  - Ribonucleoproteins, Small Nuclear/chemistry/*genetics
MH  - Sequence Alignment
MH  - Spliceosomes/metabolism
PMC - PMC1171676
EDAT- 1999/11/02 00:00
MHDA- 1999/11/02 00:01
CRDT- 1999/11/02 00:00
PHST- 1999/11/02 00:00 [pubmed]
PHST- 1999/11/02 00:01 [medline]
PHST- 1999/11/02 00:00 [entrez]
AID - 10.1093/emboj/18.21.6119 [doi]
PST - ppublish
SO  - EMBO J. 1999 Nov 1;18(21):6119-33. doi: 10.1093/emboj/18.21.6119.