Abstract/Details

The role of the tyrosine cluster and the walker A ATP binding motif of the protein Wzc in the production of emulsan in <i>Acinetobacter venetianus RAG-1</i>


2006 2006

Other formats: Order a copy

Abstract (summary)

Two regions of the wzc gene of Acinetobacter venetianus RAG-1 were investigated to understand their effects on the chain-length of the bioemulsifier emulsan. The Wzc protein is responsible for polymerization and export. When it is dephosphorylated, higher- molecular-weight exopolysaccharides result.

Point mutations in the walker A motif, the tyrosine autophosphorylation sites, and a combination of both were introduced into RAG-1 and the products excreted by these three variants were examined. The mutant in the autophosphorylation sites incorporated an unexpected frameshift which introduced a stop codon. The walker A mutant produced a low-molecular-weight polymer indicating that ATP binding in this region occurs through a separate mechanism than autophosphorylation on the 5-tyrosine residues. The mutant with both mutations was unable to carry out normal polymerization and export.

These results allow for further exploration of the ATP binding regulation mechanism for emulsan polymerization and the role of the N-terminus of Wzc.

Indexing (details)


Subject
Biomedical research;
Microbiology;
Molecular biology
Classification
0541: Biomedical research
0410: Microbiology
0307: Molecular biology
Identifier / keyword
Applied sciences; Biological sciences
Title
The role of the tyrosine cluster and the walker A ATP binding motif of the protein Wzc in the production of emulsan in <i>Acinetobacter venetianus RAG-1</i>
Author
Pleasant, Marielle L.
Number of pages
69
Publication year
2006
Degree date
2006
School code
0234
Source
MAI 44/06M, Masters Abstracts International
Place of publication
Ann Arbor
Country of publication
United States
ISBN
9780542727559
Advisor
Kaplan, David
University/institution
Tufts University
University location
United States -- Massachusetts
Degree
M.S.
Source type
Dissertations & Theses
Language
English
Document type
Dissertation/Thesis
Dissertation/thesis number
1436342
ProQuest document ID
304985176
Copyright
Database copyright ProQuest LLC; ProQuest does not claim copyright in the individual underlying works.
Document URL
http://search.proquest.com/docview/304985176
Access the complete full text

You can get the full text of this document if it is part of your institution's ProQuest subscription.

Try one of the following:

  • Connect to ProQuest through your library network and search for the document from there.
  • Request the document from your library.
  • Go to the ProQuest login page and enter a ProQuest or My Research username / password.