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Effects of novel peptides derived from the acidic tail of synuclein (ATS) on the aggregation and stability of fusion proteins

Authors
 Sang Myun Park  ;  Keun Jae Ahn  ;  Jongsun Kim  ;  Jeon Han Park  ;  Han Young Jung 
Citation
 PROTEIN ENGINEERING DESIGN & SELECTION, Vol.17(3) : 251-260, 2004 
Journal Title
 PROTEIN ENGINEERING DESIGN & SELECTION 
ISSN
 1741-0126 
Issue Date
2004
MeSH
Adiponectin ; Amino Acid Sequence ; Circular Dichroism ; Glutathione Transferase/metabolism ; Hot Temperature ; Intercellular Signaling Peptides and Proteins/chemistry ; Intercellular Signaling Peptides and Proteins/metabolism ; Kinetics ; Nerve Tissue Proteins/chemistry* ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism* ; Nerve Tissue Proteins/physiology* ; Peptides/chemistry* ; Peptides/genetics ; Peptides/isolation & purification ; Peptides/metabolism* ; Peptides/physiology* ; Protein Binding ; Protein Structure, Secondary ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Spectrophotometry, Ultraviolet ; Synucleins ; Tetrahydrofolate Dehydrogenase/chemistry ; Tetrahydrofolate Dehydrogenase/metabolism ; alpha-Synuclein ; gamma-Synuclein
Keywords
fusion protein ; heat-resistant proteins ; protein aggregation ; protein stability ; a-synuclein
Abstract
The acidic tail of alpha-synuclein (ATSalpha) has been shown to protect the glutathione S-transferase (GST)-ATSalpha fusion protein from environmental stresses, such as heat, pH and metal ions. In this study, we further demonstrated that the introduction of ATSalpha into other proteins, such as dehydrofolate reductase and adiponectin, renders the fusion proteins resistant to heat-induced aggregation and that the acidic tail of beta- or gamma-synuclein can also protect the fusion proteins from heat-induced aggregation. Interestingly, the heat resistance of GST-ATSalpha deletion mutants, which contain shorter peptides derived from the highly charged regions of ATSalpha, was approximately proportional to the number of added Glu/Asp residues. However, the negative charges in the ATSalpha-derived peptides appear insufficient to explain the extreme heat resistance of the fusion proteins, since polyglutamates appeared to be much less effective than the ATSalpha-derived peptides in conferring heat resistance on the fusion proteins. These results suggest that not only the negatively charged residues but also the specific amino acid sequence of ATSalpha play an important role in conferring extreme heat resistance on the fusion proteins. Furthermore, the heat-induced secondary structural changes and thermal inactivation curves of GST-ATSalpha deletion mutants indicated that the introduction of ATSalpha-derived peptides does not significantly affect the intrinsic stability of the fusion proteins
Files in This Item:
T200400946.pdf Download
DOI
10.1093/protein/gzh029
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
Park, Jeon Han(박전한) ORCID logo https://orcid.org/0000-0001-9604-3205
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/112483
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