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.
Original language | English (US) |
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Pages (from-to) | 108-117 |
Number of pages | 10 |
Journal | Experimental Cell Research |
Volume | 297 |
Issue number | 1 |
DOIs | |
State | Published - Jul 1 2004 |
Keywords
- Binding
- Heat shock proteins
- Hsp70
- MHC and processing
- Mass spectrophotometry
- Peptides
ASJC Scopus subject areas
- Cell Biology