Your browser does not support JavaScript!

Home    Λειτουργικός χαρακτηρισμός συντηρημένων περιοχών της περιοχής πρόσδεσης του υποστρώματος στην SecA  

Results - Details

Add to Basket
[Add to Basket]
Identifier 000334427
Title Λειτουργικός χαρακτηρισμός συντηρημένων περιοχών της περιοχής πρόσδεσης του υποστρώματος στην SecA
Alternative Title Functional characterization of conserved regions in the preprotein binding domain of SecA
Author Σαρδής, Μάριος-Φραντζέσκος
Thesis advisor Οικονόμου, Αναστάσιος
Abstract SecA is the motor of bacterial translocase. Its functional role is to convert chemical energy to mechanical work that facilitates and directs preprotein threading through the SecYEG embrane-embedded channel. SecA belongs to the superfamily of RNA helicases 2 (SF2). Hydrolysis of ATP takes place at the amino-terminal DEAD motor. There are two auxiliary domains that give to SecA its functional specialization; the Preprotein Binding Domain(PBD) and the C-domain. The C-domain regulates hydrolysis of ATP at the motor through a long α-helix(Scaffold Domain). The PBD is the region where preproteins are recognized by SecA. Along the PBD, there are many amino acid residues that are conserved across a wide range of different bacterial species. In this study we try to better understand the functional importance of these regions, in an effort to elucidate the mechanism of SecA-driven preprotein translocation. To achieve that we used alanine mutagenesis and we studied the resulting deficiencies. Our results demonstrate that PBD participates in the priming of SecA by SecYEG and preproteins.
Physical description 66 σ. : εικ. ; 30 εκ.
Language Greek
Issue date 2008-12-04
Collection   School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Post-graduate theses
Views 260

Digital Documents
No preview available

Download document
View document
Views : 3