Role of a-Subunit VISIT-DG Sequence Residues Ile-346 and Ile-348 in the Catalytic Sites of Escherichia Coli ATP Synthase.

<p>F₁F_O-ATP synthase is the primary source of cellular energy production in most living organisms. Malfunction of this enzyme is implicated in diseases. There are many functional motifs in and around the catalytic sites of this enzyme. One of them is the highly conserved &#945;-subunit VISIT-DG sequence that is close to the Pi binding subdomain. The questions arise "Are they involved in Pi binding? Or are they there simply for the structural integrity of the catalytic sites?" Here, &#945;Ile-346and &#945;Ile-348, two important residues of the conserved VISIT-DG sequence, are discussed. Each residue was mutated to A/R/D/Q. Growth assays in limiting glucose media and on succinate plates suggests &#945;Ile-346 and &#945;Ile-348 are critical for the normal enzymatic function (oxidative phosphorylation). And the biochemical assays do suggest both &#945;I-346 and &#945;I-348 are required to maintain catalytic site, involved in Pi binding indirectly, but &#945;I-348 plays more important role than &#945;I-346.</p>

Name thesis:degree_name

MS (Master of Science)

Level thesis:degree_level

Thesis - restricted

Discipline thesis:degree_discipline

Biology

Year dc:date.issued

2011

Author dc:creator

• Zhao, Chao

• ATP synthase
• VISIT-DG sequence
• Pi binding
• Biochemistry, Biophysics, and Structural Biology
• Life Sciences
• Molecular Biology

Statement dc:rights

• Copyright by the authors.

Repository record dc:identifier

https://dc.etsu.edu/etd/1270

OAI identifier oai:identifier

oai:dc.etsu.edu:etd-2461