This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The oxidative stress defenses of H. pylori are essential in allowing the bacterium to persist in its infection in the stomach, where it causes ulcers. An essential part of the bacterium's defense against oxidative stress is the methionine sulfoxide reductase repair enzyme, which can convert methionine sulfoxide to unmodified methionine. Previous studies have indicated that one of the enzymes that methionine sulfoxide reductase interacts with is catalase, another protein essential to the oxidative stress response pathways in H. pylori. In this subproject, we will oxidize catalase with a chemical oxidant such as hypochlorite, and then measure the amount of oxidation of each methionine side chain by mass spectrometry. We will then incubate the oxidized catalase with H. pylori methionine sulfoxide reductasae, including a mutant reductase with attenuated activity, and examine which methionines are repaired by the reductase.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR005351-21
Application #
8168899
Study Section
Special Emphasis Panel (ZRG1-IMST-A (40))
Project Start
2010-04-10
Project End
2011-01-31
Budget Start
2010-04-10
Budget End
2011-01-31
Support Year
21
Fiscal Year
2010
Total Cost
$1,685
Indirect Cost
Name
University of Georgia
Department
Type
Organized Research Units
DUNS #
004315578
City
Athens
State
GA
Country
United States
Zip Code
30602
Hannides, Angelos K; Aller, Robert C (2016) Priming effect of benthic gastropod mucus on sedimentary organic matter remineralization. Limnol Oceanogr 61:1640-1650
Revoredo, Leslie; Wang, Shengjun; Bennett, Eric Paul et al. (2016) Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family. Glycobiology 26:360-76
Zhao, Wujun; Zhu, Taotao; Cheng, Rui et al. (2016) Label-Free and Continuous-Flow Ferrohydrodynamic Separation of HeLa Cells and Blood Cells in Biocompatible Ferrofluids. Adv Funct Mater 26:3990-3998
Wu, Liang; Viola, Cristina M; Brzozowski, Andrzej M et al. (2015) Structural characterization of human heparanase reveals insights into substrate recognition. Nat Struct Mol Biol 22:1016-22
Qiu, Hong; Xiao, Wenyuan; Yue, Jingwen et al. (2015) Heparan sulfate modulates Slit3-induced endothelial cell migration. Methods Mol Biol 1229:549-55
Li, Zixuan; Moniz, Heather; Wang, Shuo et al. (2015) High structural resolution hydroxyl radical protein footprinting reveals an extended Robo1-heparin binding interface. J Biol Chem 290:10729-40
Czuchry, Diana; Desormeaux, Paul; Stuart, Melissa et al. (2015) Identification and Biochemical Characterization of the Novel ?2,3-Sialyltransferase WbwA from Pathogenic Escherichia coli Serotype O104. J Bacteriol 197:3760-8
Liu, Lin; Zha, Jingying; DiGiandomenico, Antonio et al. (2015) Synthetic Enterobacterial Common Antigen (ECA) for the Development of a Universal Immunotherapy for Drug-Resistant Enterobacteriaceae. Angew Chem Int Ed Engl 54:10953-7
Zhang, Fuming; Moniz, Heather A; Walcott, Benjamin et al. (2014) Probing the impact of GFP tagging on Robo1-heparin interaction. Glycoconj J 31:299-307
Zarnowski, Robert; Westler, William M; Lacmbouh, Ghislain Ade et al. (2014) Novel entries in a fungal biofilm matrix encyclopedia. MBio 5:e01333-14

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