Literature DB >> 24314090

The role of semidisorder in temperature adaptation of bacterial FlgM proteins.

Jihua Wang1, Yuedong Yang, Zanxia Cao, Zhixiu Li, Huiying Zhao, Yaoqi Zhou.   

Abstract

Probabilities of disorder for FlgM proteins of 39 species whose optimal growth temperature ranges from 273 K (0°C) to 368 K (95°C) were predicted by a newly developed method called Sequence-based Prediction with Integrated NEural networks for Disorder (SPINE-D). We showed that the temperature-dependent behavior of FlgM proteins could be separated into two subgroups according to their sequence lengths. Only shorter sequences evolved to adapt to high temperatures (>318 K or 45°C). Their ability to adapt to high temperatures was achieved through a transition from a fully disordered state with little secondary structure to a semidisordered state with high predicted helical probability at the N-terminal region. The predicted results are consistent with available experimental data. An analysis of all orthologous protein families in 39 species suggests that such a transition from a fully disordered state to semidisordered and/or ordered states is one of the strategies employed by nature for adaptation to high temperatures.
Copyright © 2013 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2013        PMID: 24314090      PMCID: PMC3853079          DOI: 10.1016/j.bpj.2013.10.026

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  42 in total

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Review 6.  Intrinsically unstructured proteins.

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Journal:  Trends Biochem Sci       Date:  2002-10       Impact factor: 13.807

7.  FlgM gains structure in living cells.

Authors:  Matthew M Dedmon; Chetan N Patel; Gregory B Young; Gary J Pielak
Journal:  Proc Natl Acad Sci U S A       Date:  2002-09-23       Impact factor: 11.205

Review 8.  Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar typhimurium and Escherichia coli.

Authors:  G S Chilcott; K T Hughes
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Review 9.  Intrinsically disordered protein.

Authors:  A K Dunker; J D Lawson; C J Brown; R M Williams; P Romero; J S Oh; C J Oldfield; A M Campen; C M Ratliff; K W Hipps; J Ausio; M S Nissen; R Reeves; C Kang; C R Kissinger; R W Bailey; M D Griswold; W Chiu; E C Garner; Z Obradovic
Journal:  J Mol Graph Model       Date:  2001       Impact factor: 2.518

10.  Intrinsically semi-disordered state and its role in induced folding and protein aggregation.

Authors:  Tuo Zhang; Eshel Faraggi; Zhixiu Li; Yaoqi Zhou
Journal:  Cell Biochem Biophys       Date:  2013       Impact factor: 2.194

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  1 in total

1.  Arabidopsis Heat Stress-Induced Proteins Are Enriched in Electrostatically Charged Amino Acids and Intrinsically Disordered Regions.

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Journal:  Int J Mol Sci       Date:  2018-08-03       Impact factor: 5.923

  1 in total

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