PMID- 10610776
OWN - NLM
STAT- MEDLINE
DCOM- 20000118
LR  - 20071115
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 294
IP  - 2
DP  - 1999 Nov 26
TI  - Identification, characterization and crystal structure analysis of the human
      spliceosomal U5 snRNP-specific 15 kD protein.
PG  - 515-25
AB  - The U5 small ribonucleoprotein particle (snRNP) contains various proteins
      involved in catalytic activities mediating conformational rearrangements of the
      spliceosome. We have isolated and characterized the evolutionarily highly
      conserved human U5 snRNP-specific protein U5-15kD. The crystal structure of
      U5-15kD determined at 1.4 A resolution revealed a thioredoxin-like fold and
      represents the first structure of a U5 snRNP-specific protein known so far. With 
      respect to human thioredoxin the U5-15kD protein contains 37 additional residues 
      causing structural changes which most likely form putative binding sites for
      other spliceosomal proteins or RNA. Moreover, a novel intramolecular disulfide
      bond replaces the canonical one found in the thioredoxin family. Even though
      U5-15kD appears to lack protein disulfide isomerase activity, it is strictly
      required for pre-mRNA splicing in vivo as we demonstrate by genetic depletion of 
      its ortholog in Saccharomyces cerevisiae. Our data suggest that the previously
      reported involvement of its Schizosaccharomyces pombe ortholog Dim1p in cell
      cycle regulation is a consequence of its essential role in pre-mRNA splicing.
CI  - Copyright 1999 Academic Press.
FAU - Reuter, K
AU  - Reuter K
AD  - Institut fur Molekularbiologie und Tumorforschung, Universitat Marburg, 35037,
      Germany.
FAU - Nottrott, S
AU  - Nottrott S
FAU - Fabrizio, P
AU  - Fabrizio P
FAU - Luhrmann, R
AU  - Luhrmann R
FAU - Ficner, R
AU  - Ficner R
LA  - eng
SI  - GENBANK/AF146373
SI  - PDB/1QGV
SI  - PDB/R1QGVSF
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA, Messenger)
RN  - 0 (Ribonucleoprotein, U5 Small Nuclear)
RN  - 0 (Schizosaccharomyces pombe Proteins)
RN  - 0 (dim1 protein, S pombe)
RN  - 52500-60-4 (Thioredoxins)
RN  - 63231-63-0 (RNA)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cell Cycle Proteins/genetics/metabolism
MH  - Cloning, Molecular
MH  - Crystallography, X-Ray
MH  - Fungal Proteins/genetics/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - RNA/metabolism
MH  - RNA Precursors/genetics
MH  - RNA Splicing
MH  - RNA, Messenger/genetics
MH  - Ribonucleoprotein, U5 Small Nuclear/*genetics/*metabolism
MH  - *Schizosaccharomyces pombe Proteins
MH  - Thioredoxins/chemistry
EDAT- 1999/12/28 00:00
MHDA- 1999/12/28 00:01
CRDT- 1999/12/28 00:00
PHST- 1999/12/28 00:00 [pubmed]
PHST- 1999/12/28 00:01 [medline]
PHST- 1999/12/28 00:00 [entrez]
AID - 10.1006/jmbi.1999.3258 [doi]
AID - S0022-2836(99)93258-8 [pii]
PST - ppublish
SO  - J Mol Biol. 1999 Nov 26;294(2):515-25. doi: 10.1006/jmbi.1999.3258.