Abstract:
:To improve chemical cross-linking of proteins coupled with mass spectrometry (CXMS), we developed a lysine-targeted enrichable cross-linker containing a biotin tag for affinity purification, a chemical cleavage site to separate cross-linked peptides away from biotin after enrichment, and a spacer arm that can be labeled with stable isotopes for quantitation. By locating the flexible proteins on the surface of 70S ribosome, we show that this trifunctional cross-linker is effective at attaining structural information not easily attainable by crystallography and electron microscopy. From a crude Rrp46 immunoprecipitate, it helped identify two direct binding partners of Rrp46 and 15 protein-protein interactions (PPIs) among the co-immunoprecipitated exosome subunits. Applying it to E. coli and C. elegans lysates, we identified 3130 and 893 inter-linked lysine pairs, representing 677 and 121 PPIs. Using a quantitative CXMS workflow we demonstrate that it can reveal changes in the reactivity of lysine residues due to protein-nucleic acid interaction.
journal_name
Elifejournal_title
eLifeauthors
Tan D,Li Q,Zhang MJ,Liu C,Ma C,Zhang P,Ding YH,Fan SB,Tao L,Yang B,Li X,Ma S,Liu J,Feng B,Liu X,Wang HW,He SM,Gao N,Ye K,Dong MQ,Lei Xdoi
10.7554/eLife.12509subject
Has Abstractpub_date
2016-03-08 00:00:00issn
2050-084Xjournal_volume
5pub_type
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