PMID- 10373544
OWN - NLM
STAT- MEDLINE
DCOM- 19990722
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 7
DP  - 1999 Jul
TI  - Cloning and characterization of two evolutionarily conserved subunits (TFIIIC102 
      and TFIIIC63) of human TFIIIC and their involvement in functional interactions
      with TFIIIB and RNA polymerase III.
PG  - 4944-52
AB  - Human transcription factor IIIC (hTFIIIC) is a multisubunit complex that mediates
      transcription of class III genes through direct recognition of promoters (for
      tRNA and virus-associated RNA genes) or promoter-TFIIIA complexes (for the 5S RNA
      gene) and subsequent recruitment of TFIIIB and RNA polymerase III. We describe
      the cognate cDNA cloning and characterization of two subunits (hTFIIIC63 and
      hTFIIIC102) that are present within a DNA-binding subcomplex (TFIIIC2) of TFIIIC 
      and are related in structure and function to two yeast TFIIIC subunits (yTFIIIC95
      and yTFIIIC131) previously shown to interact, respectively, with the promoter (A 
      box) and with a subunit of yeast TFIIIB. hTFIIIC63 and hTFIIIC102 show parallel
      in vitro interactions with the homologous human TFIIIB and RNA polymerase III
      components, as well as additional interactions that may facilitate both TFIIIB
      and RNA polymerase III recruitment. These include novel interactions of hTFIIIC63
      with hTFIIIC102, with hTFIIIB90, and with hRPC62, in addition to the
      hTFIIIC102-hTFIIIB90 and hTFIIIB90-hRPC39 interactions that parallel the
      previously described interactions in yeast. As reported for yTFIIIC131,
      hTFIIIC102 contains acidic and basic regions, tetratricopeptide repeats (TPRs),
      and a helix-loop-helix domain, and mutagenesis studies have implicated the TPRs
      in interactions both with hTFIIIC63 and with hTFIIIB90. These observations
      further document conservation from yeast to human of the structure and function
      of the RNA polymerase III transcription machinery, but in addition, they provide 
      new insights into the function of hTFIIIC and suggest direct involvement in
      recruitment of both TFIIIB and RNA polymerase III.
FAU - Hsieh, Y J
AU  - Hsieh YJ
AD  - Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New
      York, New York 10021, USA.
FAU - Wang, Z
AU  - Wang Z
FAU - Kovelman, R
AU  - Kovelman R
FAU - Roeder, R G
AU  - Roeder RG
LA  - eng
SI  - GENBANK/AF133123
SI  - GENBANK/AF133124
GR  - CA42567/CA/NCI NIH HHS/United States
PT  - Journal Article
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 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (TATA-Box Binding Protein)
RN  - 0 (Transcription Factor TFIIIB)
RN  - 0 (Transcription Factors)
RN  - 0 (Transcription Factors, TFIII)
RN  - 0 (transcription factor TFIIIC)
RN  - EC 2.7.7.6 (RNA Polymerase III)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - DNA, Complementary
MH  - DNA-Binding Proteins/metabolism
MH  - *Evolution, Molecular
MH  - Humans
MH  - Molecular Sequence Data
MH  - RNA Polymerase III/*metabolism
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - TATA-Box Binding Protein
MH  - Transcription Factor TFIIIB
MH  - Transcription Factors/*genetics/*metabolism
MH  - *Transcription Factors, TFIII
PMC - PMC84305
EDAT- 1999/06/22 00:00
MHDA- 1999/06/22 00:01
CRDT- 1999/06/22 00:00
PHST- 1999/06/22 00:00 [pubmed]
PHST- 1999/06/22 00:01 [medline]
PHST- 1999/06/22 00:00 [entrez]
AID - 10.1128/mcb.19.7.4944 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Jul;19(7):4944-52. doi: 10.1128/mcb.19.7.4944.