Unexpected Trypsin Cleavage at Ubiquitinated Lysines | Zendy

Meghan C. Burke | Zendy; Yan Wang | Zendy; Amanda E. Lee | Zendy; Emma K. Dixon | Zendy; Carlos A. Castañeda | Zendy; David Fushman | Zendy; Catherine Fenselau | Zendy

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Unexpected Trypsin Cleavage at Ubiquitinated Lysines

Author(s) -

Meghan C. Burke,

Yan Wang,

Amanda E. Lee,

Emma K. Dixon,

Carlos A. Castañeda,

David Fushman,

Catherine Fenselau

Publication year - 2015

Publication title -

analytical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.117

H-Index - 332

eISSN - 1520-6882

pISSN - 0003-2700

DOI - 10.1021/acs.analchem.5b01960

Subject(s) - chemistry , cleavage (geology) , trypsin , ubiquitin , biophysics , biochemistry , enzyme , geotechnical engineering , fracture (geology) , engineering , gene , biology

Unexpected tryptic cleavage has been characterized at modified K48 residues in polyubiquitins. In particular, the tryptic products of all seven of the lysine-linked dimers of ubiquitin and of three trimers-linear Ub-(48)Ub-(48)Ub, linear Ub-(63)Ub-(63)Ub, and the branched trimer [Ub]2-(6,48)Ub-have been analyzed. In addition to the peptide products expected under commonly used tryptic conditions, we observe that peptides are formed with an unexpected ε-glycinylglycinyl-Lys carboxyl terminus when the site of linkage is Lys48. Trypsin from three different commercial sources exhibited this aberration. Initial cleavage at R74 is proposed in a distal ubiquitin to produce a glycinylglycinyl-lysine residue which is bound by trypsin.

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