Modulation of Alpha-Subunit VISIT-DG Sequence Residues Ser-347, Gly-351 and Thr-349 in the Catalytic Sites of <em>Escherichia coli</em> ATP Synthase.

<p>Binding of inorganic phosphate (P_i) in ATP synthase catalytic sites is a crucial step for the synthesis of adenosine-5'-triphosphate (ATP). ATP is the fundamental means of cellular energy in almost every organism, and in order to gain insight into the regulation of ATP catalysis, critical amino acid residues responsible for binding P_i must be identified. Here, we investigate the role of highly conserved &#945;-subunit VISIT-DG sequence residues &#945;Ser-347, &#945;Gly-351, and &#945;Thr-349 in P_i binding. Mutations &#945;S347A/Q, &#945;G351Q, &#945;T349A/D/R, βR182A, and &#945;T349R/&#946;R182A were generated via site directed mutagenesis. Results from biochemical assays showed that &#945;Ser-347 is required for transition state stabilization and P_i binding whereas &#945;Gly-351 is only indirectly involved in P_i binding and most likely maintains structural integrity of the catalytic site. Results from preliminary experiments on &#945;Thr-349 mutants suggest that the residue may be involved in P_i binding; however, further investigation is required to fully test this hypothesis.</p>

Name thesis:degree_name

MS (Master of Science)

Level thesis:degree_level

Thesis - unrestricted

Discipline thesis:degree_discipline

Biology

Year dc:date.issued

2010

Author dc:creator

• Brudecki, Laura Elaine

• Phosphate binding
• VISIT-DG
• Escherichia coli
• ATP synthase
• Bacteriology
• Life Sciences
• Microbiology

Statement dc:rights

• Copyright by the authors.

Repository record dc:identifier

https://dc.etsu.edu/etd/1773

OAI identifier oai:identifier

oai:dc.etsu.edu:etd-3128