PMID- 10385517
OWN - NLM
STAT- MEDLINE
DCOM- 19990802
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 7
DP  - 1999 Jun 28
TI  - Combined biochemical and electron microscopic analyses reveal the architecture of
      the mammalian U2 snRNP.
PG  - 1355-68
AB  - The 17S U2 small nuclear ribonucleoprotein particle (snRNP) represents the active
      form of U2 snRNP that binds to the pre-mRNA during spliceosome assembly. This
      particle forms by sequential interactions of splicing factors SF3b and SF3a with 
      the 12S U2 snRNP. We have purified SF3b and the 15S U2 snRNP, an intermediate in 
      the assembly pathway, from HeLa cell nuclear extracts and show that SF3b consists
      of four subunits of 49, 130, 145, and 155 kD. Biochemical analysis indicates that
      both SF3b and the 12S U2 snRNP are required for the incorporation of SF3a into
      the 17S U2 snRNP. Nuclease protection studies demonstrate interactions of SF3b
      with the 5' half of U2 small nuclear RNA, whereas SF3a associates with the 3'
      portion of the U2 snRNP and possibly also interacts with SF3b. Electron
      microscopy of the 15S U2 snRNP shows that it consists of two domains in which the
      characteristic features of isolated SF3b and the 12S U2 snRNP are conserved.
      Comparison to the two-domain structure of the 17S U2 snRNP corroborates the
      biochemical results in that binding of SF3a contributes to an increase in size of
      the 12S U2 domain and possibly induces a structural change in the SF3b domain.
FAU - Kramer, A
AU  - Kramer A
AD  - Departement de Biologie Cellulaire, Universite de Geneve, CH-1211 Geneve 4,
      Switzerland. angela.kraemer@cellbio.unige.ch
FAU - Gruter, P
AU  - Gruter P
FAU - Groning, K
AU  - Groning K
FAU - Kastner, B
AU  - Kastner B
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Anion Exchange Resins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (RNA Splicing Factors)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Resins, Synthetic)
RN  - 0 (Ribonucleoprotein, U2 Small Nuclear)
RN  - 0 (SF3B1 protein, human)
RN  - 0 (splicing factor 3a)
RN  - 83453-40-1 (Mono Q)
RN  - EC 3.1.31.1 (Micrococcal Nuclease)
SB  - IM
MH  - Anion Exchange Resins
MH  - Base Sequence
MH  - Chromatography, Liquid
MH  - HeLa Cells
MH  - Humans
MH  - Micrococcal Nuclease
MH  - Microscopy, Electron
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/analysis/isolation & purification/metabolism
MH  - Nucleic Acid Conformation
MH  - Phosphoproteins/chemistry/isolation & purification/metabolism/ultrastructure
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Conformation
MH  - RNA Splicing Factors
MH  - RNA-Binding Proteins/chemistry/isolation & purification/metabolism
MH  - Resins, Synthetic
MH  - Ribonucleoprotein, U2 Small Nuclear/chemistry/isolation &
      purification/metabolism/*ultrastructure
MH  - Spliceosomes/*chemistry/metabolism/ultrastructure
PMC - PMC2133165
EDAT- 1999/06/29 00:00
MHDA- 1999/06/29 00:01
CRDT- 1999/06/29 00:00
PHST- 1999/06/29 00:00 [pubmed]
PHST- 1999/06/29 00:01 [medline]
PHST- 1999/06/29 00:00 [entrez]
AID - 10.1083/jcb.145.7.1355 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Jun 28;145(7):1355-68. doi: 10.1083/jcb.145.7.1355.