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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
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Σαρδής, Μάριος-Φραντζέσκος
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Thesis advisor
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Οικονόμου, Αναστάσιος
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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.
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Physical description |
66 σ. : εικ. ; 30 εκ. |
Language |
Greek |
Issue date |
2008-12-04 |
Collection
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School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses
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Type of Work--Post-graduate theses
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Views |
260 |