Abstract:
:The molecular chaperone SecB binds to hydrophobic sections of unfolded secretory proteins and thereby prevents their premature folding prior to secretion by the translocase of Escherichia coli. Here, we have investigated the effect of the single-residue mutation of leucine 42 to arginine (L42R) centrally positioned in the polypeptide binding pocket of SecB on its chaperonin function. The mutant retains its tetrameric structure and SecA targeting function but is defective in its holdase activity. Isothermal titration calorimetry and single-molecule optical tweezer studies suggest that the SecB(L42R) mutant exhibits a reduced polypeptide binding affinity allowing for partial folding of the bound polypeptide chain rendering it translocation-incompetent.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Bechtluft P,Kedrov A,Slotboom DJ,Nouwen N,Tans SJ,Driessen AJdoi
10.1021/bi902051esubject
Has Abstractpub_date
2010-03-23 00:00:00pages
2380-8issue
11eissn
0006-2960issn
1520-4995journal_volume
49pub_type
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