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.
Wen
Z
Z
College of Light Industry and Food Sciences, Key Lab of Fermentation and Enzyamtic Engineering, South China University of Technology, Guangzhou 510640, China.
Wang
Y
Y
Xu
X
X
Yang
B
B
Li
W
W
Xie
M
M
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015246:Deoxyribonuclease EcoRI / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D050888:Heat-Shock Proteins, Small / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000737:chemistry; D048229:Sulfolobus solfataricus / Q000235:genetics / Q000378:metabolism*
D019843:Archaeal Proteins; D050888:Heat-Shock Proteins, Small; D012965:Sodium Chloride; D015246:Deoxyribonuclease EcoRI