Literature DB >> 15504341

pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27kDa (HspB1).

Ivan S Chernik1, Olesya O Panasenko, Yi Li, Steven B Marston, Nikolai B Gusev.   

Abstract

The effect of pH on the structure of recombinant chicken Hsp24, human Hsp27 and their 3D mutants mimicking phosphorylation at Ser15, Ser77/78, and Ser81/82 was analyzed. Circular dichroism and fluorescent spectroscopy indicate that changes of pH in the range 6.0-7.5 weakly affected the secondary and tertiary structure of the wild type proteins, but induced noticeable changes in the structure of their 3D mutants. According to size-exclusion chromatography and analytical ultracentrifugation variation of pH-induced pronounced changes in the quaternary structure of small heat shock proteins and acidification resulted in accumulation of large oligomers of Hsp24/27. It is concluded that small changes of pH strongly affect the quaternary structure of small heat shock proteins and by this means can influence their functioning in the cell.

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Year:  2004        PMID： 15504341     DOI： 10.1016/j.bbrc.2004.09.176

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  8 in total

1.  Regulation of small heat-shock proteins by hetero-oligomer formation.

Authors:  Evgeny V Mymrikov; Mareike Riedl; Carsten Peters; Sevil Weinkauf; Martin Haslbeck; Johannes Buchner
Journal:  J Biol Chem       Date:  2019-11-25       Impact factor: 5.157

Review 2.  Heat shock protein 27: its potential role in vascular disease.

Authors:  Gordon Ferns; Sedigheh Shams; Shahida Shafi
Journal:  Int J Exp Pathol       Date:  2006-08       Impact factor: 1.925

3.  pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.

Authors:  Amanda F Clouser; Rachel E Klevit
Journal:  Cell Stress Chaperones       Date:  2017-03-22       Impact factor: 3.667

4.  Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function.

Authors:  David Hayes; Vanessa Napoli; Andrew Mazurkie; Walter F Stafford; Philip Graceffa
Journal:  J Biol Chem       Date:  2009-04-30       Impact factor: 5.157

5.  Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function.

Authors:  Andreas Unger; Lisa Beckendorf; Pierre Böhme; Rudolf Kley; Marion von Frieling-Salewsky; Hanns Lochmüller; Rolf Schröder; Dieter O Fürst; Matthias Vorgerd; Wolfgang A Linke
Journal:  Acta Neuropathol Commun       Date:  2017-09-15       Impact factor: 7.801

6.  Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states.

Authors:  Amanda F Clouser; Hannah Er Baughman; Benjamin Basanta; Miklos Guttman; Abhinav Nath; Rachel E Klevit
Journal:  Elife       Date:  2019-10-01       Impact factor: 8.140

7.  Using RT-PCR and glutathione level to study the effect of follicular fluid on in vitro maturation and gene expression of sheep oocytes.

Authors:  M Al-Mutary; M Al-Ghadi; A Al-Himaidi; D Iwamoto; Y Al-Anazi; A Ammari; J Ahmad; A Al-Khedhairy
Journal:  Saudi J Biol Sci       Date:  2018-01-31       Impact factor: 4.219

8.  Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins.

Authors:  Sebastian Kötter; Andreas Unger; Nazha Hamdani; Patrick Lang; Matthias Vorgerd; Luitgard Nagel-Steger; Wolfgang A Linke
Journal:  J Cell Biol       Date:  2014-01-13       Impact factor: 10.539
  8 in total

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