Dynamic and Structural Analysis of Hyperthermophilic Cold Shock Protein Stability

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  • MOTONO Chie
    Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST)
  • GROMIHA M. Michael
    Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST)

Bibliographic Information

Other Title
  • 分子動力学計算による超好熱菌由来タンパク質の安定性の解析
  • ブンシ ドウリキガク ケイサン ニ ヨル チョウコウネツキン ユライ タンパクシツ ノ アンテイセイ ノ カイセキ

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Description

The cold shock protein (CSP) from hyperthermophile Thermotoga maritima (TmCSP) is only marginally stable at 353 K, the optimum environmental temperature Topt for T. maritima. In comparison, homologous CSPs from mesophilic E. coli and B. subtilis are at least 5 times more stable at 310 K, the Topt for the mesophiles. Yet at room temperature, TmCSP is more stable than its homologues. This unique observation suggests that kinetic, rather than thermodynamic, barriers towards unfolding might help TmCSP native structure at high temperatures. High temperature (600 K) complete unfolding MD simulations of TmCSP support our hypothesis and reveal an unfolding scheme unique to TmCSP. For all the studied homologues of TmCSP, the unfolding process first starts at the C-terminal region and the N-terminal region unfolds last. But for TmCSP, unfolding starts at both terminals simultaneously. In TmCSP, the C-terminal region is better fortified and has better interactions with the N-terminal region due to the charged residues, R2, E47, E49, H61, K63 and E66, being in spatial vicinity. The electrostatic interactions among these residues are unique to TmCSP. Consistently, the room temperature MD simulations show that TmCSP is more rigid at its N- and C- termini as compared to its homologues from E. coli, B. subtilis and B. caldolyticus.<br>

Journal

  • KOBUNSHI RONBUNSHU

    KOBUNSHI RONBUNSHU 67 (3), 151-163, 2010

    The Society of Polymer Science, Japan

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