PMID- 10207079
OWN - NLM
STAT- MEDLINE
DCOM- 19990518
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 5
DP  - 1999 May
TI  - Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP
      binding to histone pre-mRNA.
PG  - 3561-70
AB  - The 3' end of histone mRNA is formed by an endonucleolytic cleavage of the
      primary transcript after a conserved stem-loop sequence. The cleavage reaction
      requires at least two trans-acting factors: the stem-loop binding protein (SLBP),
      which binds the stem-loop sequence, and the U7 snRNP that interacts with a
      sequence downstream from the cleavage site. Removal of SLBP from a nuclear
      extract abolishes 3'-end processing, and the addition of recombinant SLBP
      restores processing activity of the depleted extract. To determine the regions of
      human SLBP necessary for 3' processing, various deletion mutants of the protein
      were tested for their ability to complement the SLBP-depleted extract. The entire
      N-terminal domain and the majority of the C-terminal domain of human SLBP are
      dispensable for processing. The minimal protein that efficiently supports
      cleavage of histone pre-mRNA consists of 93 amino acids containing the
      73-amino-acid RNA-binding domain and 20 amino acids located immediately next to
      its C terminus. Replacement of these 20 residues with an unrelated sequence in
      the context of the full-length SLBP reduces processing >90%.
      Coimmunoprecipitation experiments with the anti-SLBP antibody demonstrated that
      SLBP and U7 snRNP form a stable complex only in the presence of pre-mRNA
      substrates containing a properly positioned U7 snRNP binding site. One role of
      SLBP is to stabilize the interaction of the histone pre-mRNA with U7 snRNP.
FAU - Dominski, Z
AU  - Dominski Z
AD  - Department of Biochemistry and Biophysics, University of North Carolina, Chapel
      Hill, North Carolina 27599, USA.
FAU - Zheng, L X
AU  - Zheng LX
FAU - Sanchez, R
AU  - Sanchez R
FAU - Marzluff, W F
AU  - Marzluff WF
LA  - eng
GR  - R01 GM029832/GM/NIGMS NIH HHS/United States
GR  - GM29832/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Histones)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Ribonucleoproteins, Small Nuclear)
RN  - 0 (SLBP protein, human)
RN  - 0 (Slbp protein, mouse)
RN  - 0 (mRNA Cleavage and Polyadenylation Factors)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Histones/*genetics
MH  - Humans
MH  - Mice
MH  - Mutation
MH  - *Nuclear Proteins
MH  - Nucleic Acid Conformation
MH  - Protein Binding
MH  - RNA Precursors/*genetics
MH  - RNA Processing, Post-Transcriptional/genetics
MH  - RNA-Binding Proteins/genetics/*metabolism
MH  - Recombinant Proteins/genetics
MH  - Ribonucleoproteins, Small Nuclear/*metabolism
MH  - Sequence Deletion
MH  - *mRNA Cleavage and Polyadenylation Factors
PMC - PMC84148
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1128/mcb.19.5.3561 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 May;19(5):3561-70. doi: 10.1128/mcb.19.5.3561.