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J. Biol. Chem., Vol. 282, Issue 28, 20667-20675, July 13, 2007

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Structure of an Atypical Orphan Response Regulator Protein Supports a New Phosphorylation-independent Regulatory Mechanism^*

Eunmi Hong, Hyang Mi Lee^¶, Hyunsook Ko^||, Dong-Uk Kim^¶, Byoung-Young Jeon, Jinwon Jung, Joon Shin, Sung-Ah Lee^||, Yangmee Kim^||1, Young Ho Jeon^**, Chaejoon Cheong^**, Hyun-Soo Cho^¶2, and Weontae Lee³

From the Department of Biochemistry and HTSD-NMR & Application NRL, Yonsei University, Seoul 120-749, the ^¶Department of Biology and Protein Network Research Center, Yonsei University, the ^||Department of Bioscience and Biotechnology and Brain Korea 21, Division of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, and the ^**Magnetic Resonance Team, Korea Basic Science Institute (KBSI), Ochang, Chungbuk 363-883, Korea

Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A new type of response regulator, hp1043 (HP-RR) from Helicobacter pylori, has been recently identified. HP-RR is essential for cell growth and does not require the well known phosphorelay scheme. Unphosphorylated HP-RR binds specifically to its own promoter (P₁₀₄₃) and autoregulates the promoter of the tlpB gene (P_tlpB). We have determined the structure of HP-RR by NMR and x-ray crystallography, revealing a symmetrical dimer with two functional domains. The molecular topology resembles that of the OmpR/PhoB subfamily, however, the symmetrical dimer is stable even in the unphosphorylated state. The dimer interface, formed by three secondary structure elements (4-5-5), resembles that of the active, phosphorylated forms of ArcA and PhoB. Several conserved residues of the HP-RR dimeric interface deviate from the OmpR/PhoB subfamily, although there are similar salt bridges and hydrophobic patches within the interface. Our findings reveal how a new type of response regulator protein could function as a cell growth-associated regulator in the absence of post-translational modification.

Received for publication, September 26, 2006 , and in revised form, April 17, 2007.

The atomic coordinates and structure factors (code 2HQN, 2HQO, 2HQR, and 2PLN) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by the Korea Science and Engineering Foundation (KOSEF) through the National Research Laboratory Program funded by the Ministry of Science and Technology (M1-0203-00-0020) and the Protein Network Research Center at Yonsei University (R112000078010010) and in part by the Brain Korea 21(BK21) program, the Basic Science Research Program (to C. C.) from the Ministry of Science and Technology of the Republic of Korea and the NMR Research Program (to Y. H. J.) from the Korea Basic Science Institute, and Korea Research Foundation Grants KRF-2004-005-C00112 and R08-2004-000-10403-02-004 funded by the Korean Government (to H. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by Molecular and Cellular BioDiscovery Research Program Grant M10301030001-05N0103-00110 from the Ministry of Science and Technology.

² To whom correspondence may be addressed. E-mail: hscho8{at}yonsei.ac.kr.

³ To whom correspondence may be addressed: Dept. of Biochemistry, College of Science, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul 120-749, Korea. Tel.: 82-2-2123-2706; Fax: 82-2-363-2706; E-mail: wlee{at}spin.yonsei.ac.kr.

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