Divalent Metal Ion Binding to the Response Regulator YycFN Studied by NMR Spectroscopy

doi:10.11938/cjmr20160107

Abstract

Abstract:

YycGF, originally identified in Bacillus subtilis, is recognized as a crucial two-component signal transduction system closely associated with cell viability. It is highly conserved in low G+C Gram-positive bacteria, including Staphylococcus aureus, Streptococcus pneumoniae and other human pathogens. The histidine kinase (HK) YycG senses extracellular or intracellular signals and phosphorylates its cognate response regulator (RR) YycF, which in turn recognizes sequence specific regions on the bacterial chromosome and regulates the expression of certain genes. The presence of a divalent metal ion is essential for phosphoryl group transfer. Here, we presented a metal ion binding study of the response regulator YycF (YycF_N) from Bacillus subtilis using NMR spectroscopy. The metal ions Ca²⁺ and Mg²⁺ induced severe chemical shift changes in YycF backbone resonances, involving mainly the Asp9, Asp16 and Asp53 residues. Furthermore, the binding affinities of Ca²⁺ and Mg²⁺ with YycF_N were compared. The results provide important clues for understanding the conformational change of YycF_N upon metal ion binding before its phosphorylation.

Key words: NMR, metal ions, interaction, YycF_N

CLC Number:

O482.53

LIU Ting, LIU Mai-li, JIANG Ling. Divalent Metal Ion Binding to the Response Regulator YycF_N Studied by NMR Spectroscopy[J]. Chinese Journal of Magnetic Resonance, 2016, 33(1): 77-88.

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Divalent Metal Ion Binding to the Response Regulator YycF_N Studied by NMR Spectroscopy

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