Recent Papers Published by Graduate Students

A University of Michigan and University of Oxford collaboration recently earned front page attention in the Royal Society of Chemistry’s journal by revealing the potential for using sunlight to efficiently convert the greenhouse gas, carbon dioxide (CO2), into storable fuels. Led by BioChem Professor Stephen Ragsdale, former BioChem graduate student Dr. Elizabeth Pierce, and Oxford Professor Fraser Armstrong, the collaboration promises to extend the use of solar energy beyond generation of electricity to the creation of storable solar fuels. The team has developed a hybrid device that contains a metal oxide nanoparticle that interacts with the enzyme carbon monoxide dehydrogenase and reacts to visible light using a ruthenium bipyridyl photosensitizer. This device functions as a highly active and reversible catalyst that can use sunlight to photo-reduce the relatively inert CO2 to methanol for use in fuel cells and carbon monoxide for conversion into liquid fuels.

Read more on the team’s work, including its earlier coverage in the Journal of the American Chemical Society.

Graduate student Chase Weidmann is listed listed as first author on Drosophila Pumilio Protein Contains Multiple Autonomous Repression Domains That Regulate mRNAs Independently of Nanos and Brain Tumor, written with his mentor Aaron Goldstrohm. Their findings suggest that PUF proteins have evolved new regulatory functions through protein sequences appended to their conserved PUF repeat RNA-binding domains. Read the abstract for this Molecular and Cellular Biology paper here PMID: 22064486

Posted 12/11

Valentin Cracan, is a student in Ruma Banerjee's lab, current interest is the elucidation of a newly discovered radical B12 enzyme, isobutyryl-CoA mutase, which is fused to a GTP-dependent chaperone, His paper, IcmF Is a Fusion between the Radical B12 Enzyme Isobutyryl-CoA Mutase and Its G-protein Chaperone, was published in the October, 2009 issue of the Journal of Biological Chemistry. It can be read at JBC.

Sean Ferris, is a student in Randal J. Kaufman's lab, where they are interested in protein folding and misfolding in cells, specifically in the endoplasmic reticulum (ER). A cellular demand for protein exceeding the protein-folding capacity of the ER results in a situation known as ER stress. His paper, Generation and phenotyping of mCd59a and mCd59b double-knockout mice, was published in February, 2009 issue of American Journal of Hematology. For it, see AJH.

Nirupama Gupta, is a student in Stephen Ragsdale's lab. Gupta is interested in how Cysteine synthase (Cys11) plays a dual role in maintaining the correct structure for DNA binding and in redox regulation of CprK. Her paper, Dual Roles of an Essential Cysteine Residue in Activity of a Redox-regulated Bacterial Transcriptional Activator, was published in the October, 2008 issue of the Journal of Biological Chemistry. It can be read at JBC.

Corissa Lamphear, is a student in Carol Fierke's lab, where her interest is how a better understanding of the molecular recognition of substrates performed by FTase will aid in both designing new FTase inhibitors as therapeutic agents and characterizing proteins involved in prenylation-dependent cellular pathways. Her paper, Context-Dependent Substrate Recognition by Protein Farnesyltransferase†, was published in the February, 2009 issue of the Biochemistry. It can be read at Biochemistry.

Rev-erbβ is a heme-binding nuclear hormone receptor that represses a broad spectrum of target genes involved in regulating metabolism, the circadian cycle and proinflammatory responses. Graduate Student Nirupama Gupta has collaborated with Professor Steve Ragdale on a paper in recent issue of the Journal of Biological Chemistry. They suggest that this thiol-disulfide redox switch is one mechanism by which oxidative stress is linked to circadian and/or metabolic imbalance; and propose that oxidative stress leads to oxidation of cysteine(s), thus releasing heme from Rev-erbβ and altering its transcriptional activity. JBC

iRhoms are inactive rhomboid-like pseudoproteases that lack essential catalytic residues. Although iRhoms are highly conserved in metazoan species, little is known about their function. In a recent issue of Developmental Cell, Graduate Student Stewart Siyan Cao and collaborator Professor Randal J. Kaufman discuss recent insights on how iRhoms regulate growth factors signaling through endoplasmic reticulum-associated protein degradation (ERAD.

Highly conserved among all sequenced metazoans, iRhoms are related to rhomboid intramembrane serine proteases, but are not active proteases, as they lack the essential catalytic residues required for serine proteases and have no proteolytic activity. Although their high degree of conservation between organisms suggests that these pseudoproteases are under evolutionary selective pressure, their functional significance is largely unknown. A previous study reported that human iRhom1 interacts with the human epidermal growth factor (EGF) when it is overexpressed in Drosophila, suggesting a possible link between an iRhom and EGFR signaling in mammals (Freeman, 2008). In a recent issue of Cell, Zettl et al. (2011) show in both Drosophila and mammalian cells that iRhoms regulate growth factor signaling (e.g., EGFR pathways) through the ER quality control machinery that function in endoplasmic reticulum-associated protein degradation (ERAD)

Cao SS, Kaufman RJ.
Comment on Cell. 2011 Apr 1;145(1):79-91.

The entire paper may be read at PubMed