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J. Biol. Chem., Vol. 275, Issue 21, 16057-16063, May 26, 2000
From the Institute for Protein Research, Osaka University, Suita,
Osaka 565-0871, Japan
The C-terminal domain of the The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB036061. The atomic coordinates and the structure factors (code 1DOQ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
The Structure and the Characteristic DNA Binding Property of
the C-terminal Domain of the RNA Polymerase
Subunit from
Thermus thermophilus*
,
subunit of the
RNA polymerase (CTD) from Escherichia coli
(Ec) regulates transcription by interacting with many kinds
of proteins and promoter upstream (UP) elements consisting of AT-rich
sequences. However, it is unclear how this system is common in all
eubacteria. We investigate the structure and properties of CTD from
an extremely thermophilic eubacterium, Thermus thermophilus
(Tt). The solution structure of Tt CTD (85 amino acids) was determined by NMR, and the interaction between
Tt CTD and DNA with different sequences was investigated by means of chemical shift perturbation experiments. The tertiary structure of Tt CTD is almost identical with that of
Ec CTD despite 32% sequence homology. However,
Tt CTD interacts with the upstream region sequence of
the promoter in the Tt 16 S ribosomal protein operon rather
than the Ec UP element DNA. The upstream region sequence of
Tt is composed of 25 base pairs with 40% AT, unlike the
Ec UP element with 80% AT. The DNA binding site in Tt CTD is located on the surface composed of helix 4 and
the loop preceding helix 4. The electric charges on this surface are not remarkably localized like those of Ec CTD.
*
This work was supported by Grant-in-aid 09480176 from the
Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: RIKEN, Harima Inst., Mikazuki-cho, Sayo-gun,
Hyogo 679-5148, Japan.
§
To whom correspondence should be addressed. Tel.: 81-6-6879-8598;
Fax: 81-6-6879-8599; E-mail: kyogoku@protein.osaka-u.ac.jp.
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