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Characterization of substrate binding to the Group II Archael Chaperonin from Methanococcus maripaludis (Mm‐Cpn)
Author(s) -
Goulet Daniel,
Knee Kelly M,
Jameel Shea,
King Jonathan Alan
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.672.6
Subject(s) - chaperonin , methanococcus , chaperone (clinical) , chemistry , protein folding , kinetics , biochemistry , biophysics , biology , gene , archaea , medicine , physics , pathology , quantum mechanics
It has been difficult to identify the features of partially folded proteins that are recognized by the Group II chaperonins. A partially folded intermediate of the two‐domain all β‐sheet human γ‐D crystallin has been well characterized. We have investigated the interactions of Methanococcus maripaludis chaperonin (Mm‐Cpn) with Human γ‐Crystallin substrates. A homologue of human chaperonins, Mm‐Cpn binds to and inhibits the aggregation of several closely related members of the Human γ?Crystallin protein family including HγD‐ and HγC‐crystallins. Although members of this protein family share a high degree of homology, Mm‐Cpn suppression of HγD aggregation is twice as efficient as the suppression of HγC aggregation. It remains unclear whether this difference in suppression efficiency is linked to sequence‐determined substrate binding kinetics or to differences in substrate aggregation kinetics. To better understand how sequence difference may affect aggregation and chaperone binding, we describe the chaperone‐induced aggregation suppression for the isolated N‐terminal and C‐terminal domains of both HγD and HγC. Supported by an NIH Roadmap Award to the Center for Protein Folding Machinery