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Identifier

uch.biology.msc//2001MST1204

Title

Μοριακός χαρακτηρισμός μιας λειτουργικά απαραίτητης αλληλουχίας της SecA

Author

Παπανίκου, Ευφροσύνη

Abstract

SecA, the motor subunit of bacterial polypeptide translocase is an RNA helicase. SecA comprises a dimerization C-domain fused to an ATPase N-domain. The N-domain is organized like the motor core of DEAD proteins and contains seven conserved DEAD helicase motifs. It encompasses two subdomains, NBD and IRA2. NBD is the nucleotide binding domain and IRA2 contains two DEAD family motifs which are essential for IRA2/NBD binding, optimal nucleotide turnover and polypeptide translocation. With the current study, we demonstrated that a conserved SecA region (motif VII), that lies between IRA2 and NBD, is essential for polypeptide translocation. Motif VII is homologous to motif III of DEAD RNA helicases. Mutants in motif VII cannot translocate polypeptides, they exhibit reduced catalytic activity and/or their folding is affected. We suggest that motif VII is important for the communication between NBD and IRA2 as well as for substrate's successful binding since it is located near the proposed PBD of SecA.

Language

Greek

Issue date

2001-12-06

Collection

School/Department--School of Sciences and Engineering--Department of Biology--Post-graduate theses

Type of Work--Post-graduate theses

Permanent Link

https://elocus.lib.uoc.gr//dlib/9/8/b/metadata-dlib-2001MST1204.tkl

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