{"id":18871,"date":"2021-08-06T13:00:50","date_gmt":"2021-08-06T17:00:50","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/?p=18871"},"modified":"2021-08-10T09:33:44","modified_gmt":"2021-08-10T13:33:44","slug":"camila-garcia-of-strahl-lab-presents-at-the-2021-summer-undergraduate-pipeline-sup-research-symposium","status":"publish","type":"post","link":"https:\/\/www.med.unc.edu\/biochem\/diversity\/camila-garcia-of-strahl-lab-presents-at-the-2021-summer-undergraduate-pipeline-sup-research-symposium\/","title":{"rendered":"Camila Garcia of Strahl lab presents at the 2021 Summer Undergraduate Pipeline (SUP) Research Symposium"},"content":{"rendered":"

On July 27, 2021, Camila Garcia of Strahl lab presents at the 6th annual 2021 Summer Undergraduate Pipeline (SUP) Research Symposium.<\/p>\n

\"up
Camila Garcia’s presentation.<\/figcaption><\/figure>\n
\"highlight
Camila Garcia’s UNC NSF SURE profile.<\/figcaption><\/figure>\n

alt text for Camila Garcia’s UNC NSF SURE profile<\/a><\/p>\n

Camila Garcia<\/p>\n

Home University: Florida Gulf Coast University<\/p>\n

Research Mentor: Brian D. Strahl, Biochemistry & Biophysics<\/p>\n

Program: SOLAR & SURE<\/p>\n

Research Title: SANT Domain Mutations that Give Insight to the Histone Binding Activity
\nThe SAGA(Spt-Ada-Gcn5-Acetyl Transferase) enzymatic complex is a highly conserved complex in eukaryotic organisms from yeast to humans. SAGA is responsible for regulating cellular processes through post-translational modifications(PTMs) on histones (e.g., acetylation, methylation). If malfunctions arise, it can result in the appearance of neurological diseases or cancer. While there\u2019s a great deal of information on the SAGA complex as a whole, the individual contribution of each protein is not well understood, this is specially true for Ada2. Ada2 protein is known for increasing the histone binding activity of the Gnc5 protein, a histone acetylator, however how this happens is unclear. From the Strahl Lab, data showed that the SANT domain of Ada2 binds both H3 and H4. Our goal this summer was to determine which amino acid residues are important for the binding of these histones to the SANT domain. Utilizing point mutations in acidic pockets of the SANT domain, we mutated the amino acids from acidic to basic and to an uncharged amino acid. Once these mutations were in the recombinant plasmid, protein purification, protein pull-down, and western blotting were performed. Preliminary results show that these mutations were not able to eliminate binding of both H3 and H4. Further studies will involve a crystal structure of the current protein to have a view on the exact binding pockets of these histones and mutate those residues.<\/p>\n

Summer Research Experience for Undergraduates in Biological Mechanisms at UNC-Chapel Hill (SURE-REU)<\/a>
\n&
\nUNC SOLAR<\/a><\/p>\n

Each year different Biochemistry and Biophysics faculty host undergraduate research fellows in their labs through various programs.<\/p>\n

Read more about this program on UNC news, Summer Undergraduate Pipeline provides research experience and opportunities explore graduate education<\/a><\/p>\n

\"24<\/p>\n","protected":false},"excerpt":{"rendered":"

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