PMID- 10095767
OWN - NLM
STAT- MEDLINE
DCOM- 19990426
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 260
IP  - 2
DP  - 1999 Mar
TI  - A novel human DNA-binding protein with sequence similarity to a subfamily of
      redox proteins which is able to repress RNA-polymerase-III-driven transcription
      of the Alu-family retroposons in vitro.
PG  - 336-46
AB  - In this study we identified a novel protein which may contribute to the
      transcriptional inactivity of Alu retroposons in vivo. A human cDNA clone
      encoding this protein (ACR1) was isolated from a human expression library using
      South-western screening with an Alu subfragment, implicated in the regulation of 
      Alu in vitro transcription and interacting with a HeLa nuclear protein
      down-regulated in adenovirus-infected cells. Bacterially expressed ACR1 is
      demonstrated to inhibit RNA polymerase III (Pol III)-dependent Alu transcription 
      in vitro but showed no repression of transcription of a tRNA gene or of a
      reporter gene under control of a Pol II promoter. ACR1 mRNA is also found to be
      down-regulated in adenovirus-infected HeLa cells, consistent with a possible
      repressor function of the protein in vivo. ACR1 is mainly (but not exclusively)
      located in cytoplasm and appears to be a member of a weakly characterized redox
      protein family having a central, highly conserved sequence motif, PGAFTPXCXXXXLP.
      One member of the family identified earlier as peroxisomal membrane protein
      (PMP)20 is known to interact in a sequence-specific manner with a yeast homolog
      of mammalian cyclosporin-A-binding protein cyclophilin, and mammalian cyclophilin
      A (an abundant ubiquitously expressed protein) is known to interact with human
      transcriptional repressor YY1, which is a major sequence-specific Alu-binding
      protein in human cells. It appears, therefore, that transcriptional silencing of 
      Alu in vivo is a result of complex interactions of many proteins which bind to
      its Pol III promoter.
FAU - Kropotov, A
AU  - Kropotov A
AD  - Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.
FAU - Sedova, V
AU  - Sedova V
FAU - Ivanov, V
AU  - Ivanov V
FAU - Sazeeva, N
AU  - Sazeeva N
FAU - Tomilin, A
AU  - Tomilin A
FAU - Krutilina, R
AU  - Krutilina R
FAU - Oei, S L
AU  - Oei SL
FAU - Griesenbeck, J
AU  - Griesenbeck J
FAU - Buchlow, G
AU  - Buchlow G
FAU - Tomilin, N
AU  - Tomilin N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Basic-Leucine Zipper Transcription Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Retroelements)
RN  - 0 (SKO1 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 2.7.7.6 (RNA Polymerase III)
SB  - IM
MH  - Adenoviridae
MH  - Alu Elements/*genetics
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Basic-Leucine Zipper Transcription Factors
MH  - DNA-Binding Proteins/genetics/*metabolism
MH  - Down-Regulation
MH  - HeLa Cells
MH  - Humans
MH  - Leucine Zippers/*genetics
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
MH  - Placenta/enzymology
MH  - RNA Polymerase III/*metabolism
MH  - Repressor Proteins/genetics/*metabolism
MH  - Retroelements/*genetics
MH  - *Saccharomyces cerevisiae Proteins
MH  - *Transcription, Genetic
EDAT- 1999/03/30 00:00
MHDA- 1999/03/30 00:01
CRDT- 1999/03/30 00:00
PHST- 1999/03/30 00:00 [pubmed]
PHST- 1999/03/30 00:01 [medline]
PHST- 1999/03/30 00:00 [entrez]
AID - 10.1046/j.1432-1327.1999.00162.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Mar;260(2):336-46. doi: 10.1046/j.1432-1327.1999.00162.x.