The protein truncation caused by fusion of PEP-1 peptide and protective roles of transduced PEP-1-MsrA in skin cells

Title
The protein truncation caused by fusion of PEP-1 peptide and protective roles of transduced PEP-1-MsrA in skin cells
Author(s)
김화영이태형[이태형]최승희[최승희]
Keywords
METHIONINE SULFOXIDE REDUCTASE; EFFICIENTLY PROTECTS; OXIDATIVE STRESS; PC12 CELLS; EXPRESSION; VIABILITY; MAMMALS; REPAIR; DAMAGE
Issue Date
201104
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.44, no.4, pp.256 - 261
Abstract
PEP-1 peptide has been used for transduction of native protein into mammalian cells. This work describes the findings that the fusion of PEP-1 to target proteins led to protein truncation likely in a non-protein-specific manner. Approximately 75% of PEP-1-MsrA fusion protein was truncated in the N-terminal region of MsrA between Lys-27 and Val-28 during expression in Escherichia coli and purification. This large protein truncation was also observed in another PEP-1 fused protein, PEP-1-MsrB2, in the N-terminal region of MsrB2. The full-length PEP-1-MsrA protein was rapidly transduced into keratinocyte cells within 15 min. The transduced PEP-1-MsrA was functionally active and could protect skin cells against oxidative stress- and ultraviolet radiation-induced cell death. Collectively, our data demonstrated the protective roles of MsrA in skin cells and, moreover, may raise a concern of protein truncation caused by fusion of PEP-1 about the general use of this peptide for protein transduction. [BMB reports 2011; 44(4): 256-261]
URI
http://hdl.handle.net/YU.REPOSITORY/25395http://dx.doi.org/10.5483/BMBRep.2011.44.4.256
ISSN
1976-6696
Appears in Collections:
의과대학 > 생화학.분자생물학교실 > Articles
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