Importance of a potential salt bridge and hydrophobic core in the function and oligomerization of a small heat shock protein

SsHSP14.1, a novel sHSP from the hyper-thermophilic archaeon Sulfolobus solfataricus (S. solfataricus), is reported herein to function to protect EcoR I from heat-induced inactivation. A predicted salt bridge and hydrophobic interactions were found to be important for this function.

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Bibliographic Details
Published inProtein and peptide letters Vol. 17; no. 6; p. 751
Main Authors Wen, Z, Wang, Y, Xu, X, Yang, B, Li, W, Xie, M
Format Journal Article
LanguageEnglish
Published Netherlands 01.06.2010
Subjects
Amino Acid Sequence
Archaeal Proteins - chemistry
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Deoxyribonuclease EcoRI - chemistry
Deoxyribonuclease EcoRI - metabolism
Enzyme Stability
Heat-Shock Proteins, Small - chemistry
Heat-Shock Proteins, Small - genetics
Heat-Shock Proteins, Small - metabolism
Hot Temperature
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Sequence Data
Mutation
Protein Binding
Protein Conformation
Protein Multimerization
Sequence Homology, Amino Acid
Sodium Chloride - chemistry
Sulfolobus solfataricus - genetics
Sulfolobus solfataricus - metabolism
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Summary:SsHSP14.1, a novel sHSP from the hyper-thermophilic archaeon Sulfolobus solfataricus (S. solfataricus), is reported herein to function to protect EcoR I from heat-induced inactivation. A predicted salt bridge and hydrophobic interactions were found to be important for this function.
ISSN:1875-5305
DOI:10.2174/092986610791190273