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KMID : 0578320130350020158
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Molecules and Cells
2013 Volume.35 No. 2 p.158 ~ p.165
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Backbone Dynamics of an Atypical Orphan Response Regulator Protein, Helicobacter pylori 1043
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Jeong Ki-Woong
Ko Hyun-Sook
Lee Sung-Ah
Hong Eun-Mi
Ko Sung-Geon
Cho Hyun-Soo
Lee Weon-Tae
Kim Yang-Mee
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Abstract
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An atypical orphan response regulator protein, HP1043 (HP-RR) in Helicobacter pylori, is proven to be essential for cell growth and does not require the well known phosphorelay scheme. HP-RR was identified as a symmetric dimer with two functional domains, an N-terminal regulatory domain (HP-RRr) and a C-terminal effector domain (HP-RRe). HP-RR is a new class of response regulator, as a phosphorylation-independent regulator. Previously, we have presented a detailed three-dimensional structure of HP-RR using NMR spectroscopy and X-ray crystallography. In this study, in order to understand the functional importance of flexibilities in HP-RRr and HP-RRe, T1, T2, heteronuclear NOE experiments have been performed and backbone dynamics of HP-RRr and HP-RRe were investigated. HP-RRr is a symmetric dimer and the interface region, α4-β5-α5 of dimer, showed high rigidity (high S2 values). Site of rearrangements associated with phosphorylation of HP-RRr (Ser75: Rex = 3.382, Ile95: Rex = 5.228) showed slow chemical exchanges. HP-RRe is composed of three α-helices flanked on two sides by anti-parallel β-sheets. Low order parameters as well as conformational exchanges in the centers of loop regions known as the DNA binding site and transcription site of HP-RRe suggested that flexibility of HP-RRe is essential for interaction with DNA. In conclusion, backbone dynamics information for HP-RR implies that structural flexibilities in HP-RRr are necessary for the phosphorylation site and the dynamic nature of HP-RRe is essential for the regulation of interaction between protein and DNA.
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KEYWORD
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backbone dynamics, C-terminal effector domain, HP1043 (HP-RR), NMR spectroscopy, N-terminal regulatory domain, spin relaxation
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