PMID- 10657236
OWN - NLM
STAT- MEDLINE
DCOM- 20000330
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 346 Pt 1
DP  - 2000 Feb 15
TI  - A novel principle for conferring selectivity to poly(A)-binding proteins:
      interdependence of two ATP synthase beta-subunit mRNA-binding proteins.
PG  - 33-9
AB  - Based on electrophoretic mobility-shift assays and UV cross-linking experiments, 
      we present evidence in the present work for the existence of two mammalian
      cytosolic proteins that selectively interact with the 3'-untranslated region of
      the mRNA coding for the catalytic beta-subunit of mitochondrial ATP synthase
      (beta-mtATPase). One of the proteins, beta-mtATPase mRNA-binding protein (BARB)1,
      is a novel poly(A)-binding protein that specifically binds the poly(A) tail of
      the beta-mtATPase transcript. BARB1 achieves this mRNA selectivity through its
      interaction with a second protein, BARB2, that binds the beta-mtATPase mRNA
      through a 22-bp element with a uridylate core, located 75 bp upstream of the
      poly(A) tail. Conversely, in the absence of BARB1, BARB2 is still able to bind
      the beta-mtATPase mRNA, but does so with lower affinity. Thus the interaction
      between BARB1 and BARB2 and beta-mtATPase mRNA involves the formation of a
      complex between the two BARB proteins. We conclude that BARB1 and BARB2
      selectively bind the 3'-untranslated region of beta-mtATPase mRNA in a novel and 
      interdependent manner. The complex between these two proteins may be involved in 
      post-transcriptional regulation of gene expression.
FAU - Andersson, U
AU  - Andersson U
AD  - The Wenner-Gren Institute, The Arrhenius Laboratories F3, Stockholm University,
      S-106 91 Stockholm, Sweden.
FAU - Antonicka, H
AU  - Antonicka H
FAU - Houstek, J
AU  - Houstek J
FAU - Cannon, B
AU  - Cannon B
LA  - eng
SI  - GENBANK/AF030559
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (3' Untranslated Regions)
RN  - 0 (Poly(A)-Binding Proteins)
RN  - 0 (RNA Probes)
RN  - 0 (RNA-Binding Proteins)
RN  - 24937-83-5 (Poly A)
RN  - E2OU15WN0N (Uridine Monophosphate)
RN  - EC 3.6.3.14 (Proton-Translocating ATPases)
SB  - IM
MH  - 3' Untranslated Regions/genetics/*metabolism
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Cytosol/chemistry
MH  - Male
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Mutation/genetics
MH  - Organ Specificity
MH  - Poly A/genetics/*metabolism
MH  - Poly(A)-Binding Proteins
MH  - Proton-Translocating ATPases/*genetics
MH  - RNA Probes/genetics/metabolism
MH  - RNA-Binding Proteins/chemistry/*metabolism
MH  - Rats
MH  - Regulatory Sequences, Nucleic Acid/genetics
MH  - Substrate Specificity
MH  - Ultraviolet Rays
MH  - Uridine Monophosphate/genetics/metabolism
PMC - PMC1220819
EDAT- 2000/02/05 09:00
MHDA- 2000/04/01 09:00
CRDT- 2000/02/05 09:00
PHST- 2000/02/05 09:00 [pubmed]
PHST- 2000/04/01 09:00 [medline]
PHST- 2000/02/05 09:00 [entrez]
PST - ppublish
SO  - Biochem J. 2000 Feb 15;346 Pt 1:33-9.