The Function of Ile-X-Ile Motif in the Oligomerization and Chaperone-Like Activity of Small Heat Shock Protein AgsA at Room Temperature

Small heat shock proteins assemble as large oligomers in vitro and exhibit ATP-independent chaperone activities. Ile-X-Ile motif is essential in both the function and oligomer formation. AgsA of Salmonella enterica serovar Typhimurium has been demonstrated to adopt large oligomeric structure and pos...

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Bibliographic Details
Published in:	Protein Journal Vol. 35; no. 6; pp. 401 - 406
Main Authors:	Zhou, Qiuhu, Shi, Xiaodong, Zhang, Kaiming, Shi, Chao, Huang, Lixin, Chang, Zhenzhan
Format:	Journal Article
Language:	English
Published:	New York Springer US 01-12-2016 Springer Springer Nature B.V
Subjects:	Adenosine triphosphatase Amino Acid Motifs Analysis Animal Anatomy Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Bioorganic Chemistry Chemistry Chemistry and Materials Science Cloning, Molecular Escherichia coli - genetics Escherichia coli - metabolism Ethylenediaminetetraacetic acid Gene Expression Heat shock proteins Heat-Shock Proteins, Small - chemistry Heat-Shock Proteins, Small - genetics Heat-Shock Proteins, Small - metabolism Histology Insulin - chemistry Microscopic analysis Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Morphology Mutants Mutation Oligomers Organic Chemistry Phosphines - chemistry Plasmids - chemistry Plasmids - metabolism Protein Aggregates Protein Multimerization Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Salmonella enterica Salmonella typhimurium - chemistry Salmonella typhimurium - genetics Salmonella typhimurium - metabolism Temperature Temperature effects Chaperone-like activity Small heat shock protein Ile-X-Ile motif Oligomerization
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Summary:	Small heat shock proteins assemble as large oligomers in vitro and exhibit ATP-independent chaperone activities. Ile-X-Ile motif is essential in both the function and oligomer formation. AgsA of Salmonella enterica serovar Typhimurium has been demonstrated to adopt large oligomeric structure and possess strong chaperone activity. Size exclusion chromatography, non-denaturing pore gradient PAGE, and negatively stain electron microscopic analysis of the various C-terminal truncated mutants were performed to investigate the role of Ile-X-Ile motif in the oligomer assembly of AgsA. By measuring the ability to prevent insulin from aggregating induced by TCEP, the chaperone-like activity of AgsA and the C-terminal truncated mutants at room temperature were determined. We found that the truncated mutants with Ile-X-Ile motif partially or fully deleted lost the ability to form large oligomers. Contrast to wild type AgsA which displayed weak chaperone-like activity, those mutants shown significantly enhanced activities at room temperature. In summary, biochemical experiment, activity assay and electron microscopic analysis suggested that Ile-X-Ile motif is essential in oligomer assembly of AgsA and might take the role of an inhibitor for its chaperone-like activity at room temperature.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1572-3887 1573-4943 1875-8355
DOI:	10.1007/s10930-016-9681-y