Proteomics shows Hsp70 does not bind peptide sequences indiscriminately in vivo |
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Authors: | Grossmann Michael E Madden Benjamin J Gao Fan Pang Yuan-Ping Carpenter John E McCormick Daniel Young Charles Y F |
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Institution: | Department of Biochemistry/Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA. |
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Abstract: | Heat shock protein 70 (Hsp70) binds peptide and has several functions that include protein folding, protein trafficking, and involvement with immune function. However, endogenous Hsp70-binding peptides had not previously been identified. Therefore, we eluted and identified several hundred endogenously bound peptides from Hsp70 using liquid chromatography ion trap mass spectrophotometry (LC-ITMS). Our work shows that the peptides are capable of binding Hsp70 as previously described. They are generally 8-26 amino acids in length and correspond to specific regions of many proteins. Through computationally assisted analysis of peptides eluted from Hsp70 we determined variable amino acid sequences, including a 5 amino acid core sequence that Hsp70 favorably binds. We also developed a computer algorithm that predicts Hsp70 binding within proteins. This work helps to define what peptides are bound by Hsp70 in vivo and suggests that Hsp70 facilitates peptide selection by aiding a funneling mechanism that is flexible but allows only a limited number of peptides to be processed. |
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Keywords: | Heat shock proteins Hsp70 Binding Mass spectrophotometry Peptides MHC and processing |
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