PMID- 10329413
OWN - NLM
STAT- MEDLINE
DCOM- 19990615
LR  - 20190612
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 258
IP  - 2
DP  - 1999 May 10
TI  - Characterization of telomere-binding activity of replication factor C large
      subunit p140.
PG  - 482-9
AB  - The large subunit of RFC (RFC p140) has been suggested to be associated with the 
      3'-end of elongating DNA primer and to recruit proliferating cell nuclear antigen
      (PCNA) onto DNA polymerase delta. Previously, we isolated a cDNA clone encoding a
      DNA-binding domain of RFC p140 as a telomeric repeat (TTAGGG)n binding protein.
      This domain was shown to have a specific affinity for the 5'-phosphate ends of a 
      telomere repeat sequence. In order to investigate the structure and function of
      RFC p140, we constructed the full-length recombinant RFC p140 as well as N-
      and/or C-terminal deleted mutants and analyzed their telomere-binding activities.
      South-Western blot and gel mobility shift analyses revealed that deletion of the 
      N- but not the C-terminal region enhances recognition of the telomeric repeat
      sequence and 5'-phosphate ends, suggesting the negative effect of the N-terminal 
      region of the RFC p140 binding to the telomeric repeat. On the other hand, the
      C-terminal truncated RFC inhibits the telomerase activity more than the
      N-terminal-deleted and full-length RFC p140. The inhibitory effect of RFC p140 on
      telomerase activity is completely diminished by both terminal deletions. Thus, a 
      certain interaction of the N- and C-terminal regions is considered to be required
      for RFC p140 to suppress telomerase activity. Taken together, these results
      suggest that both telomeric repeat-binding and telomerase inhibitory activities
      of RFC p140 are finely regulated by the intrinsic N- and C-terminal regions.
CI  - Copyright 1999 Academic Press.
FAU - Uchiumi, F
AU  - Uchiumi F
AD  - Faculty of Pharmaceutical Sciences, Science University of Tokyo, Shinjuku-ku,
      Tokyo, 162, Japan.
FAU - Watanabe, M
AU  - Watanabe M
FAU - Tanuma, S i
AU  - Tanuma Si
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (BCL2-related protein A1)
RN  - 0 (DNA Primers)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Homeodomain Proteins)
RN  - 0 (MATA1 protein, S cerevisiae)
RN  - 0 (Minor Histocompatibility Antigens)
RN  - 0 (Proto-Oncogene Proteins c-bcl-2)
RN  - 0 (Repressor Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 2.7.7.49 (Telomerase)
RN  - EC 3.6.4.- (Replication Protein C)
SB  - IM
MH  - Aging/genetics
MH  - Base Sequence
MH  - DNA Primers
MH  - DNA-Binding Proteins/chemistry/*metabolism
MH  - HeLa Cells
MH  - *Homeodomain Proteins
MH  - Humans
MH  - Jurkat Cells
MH  - Minor Histocompatibility Antigens
MH  - *Proto-Oncogene Proteins c-bcl-2
MH  - Replication Protein C
MH  - *Repressor Proteins
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Deletion
MH  - Telomerase/antagonists & inhibitors
MH  - *Telomere
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - S0006291X99905892 [pii]
AID - 10.1006/bbrc.1999.0589 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 May 10;258(2):482-9. doi:
      10.1006/bbrc.1999.0589.