Scholars@Duke
Gustavo M. Silva

Gustavo M. Silva

Associate Professor of Biology
Biology
gustavo.silva@duke.edu
130 Science Drive, Box 90338, Durham, NC 27708
130 Science Drive, 3103 French, Durham, NC 27708

Selected Publications

The ubiquitin conjugase Rad6 mediates ribosome pausing during oxidative stress.

Journal Article Cell reports · November 2023 Oxidative stress causes K63-linked ubiquitination of ribosomes by the E2 ubiquitin conjugase Rad6. How Rad6-mediated ubiquitination of ribosomes affects translation, however, is unclear. We therefore perform Ribo-seq and Disome-seq in Saccharomyces cerevis ... Full text Cite

The central role of translation elongation in response to stress.

Journal Article Biochemical Society transactions · June 2023 Protein synthesis is essential to support homeostasis, and thus, must be highly regulated during cellular response to harmful environments. All stages of translation are susceptible to regulation under stress, however, the mechanisms involved in translatio ... Full text Cite

Redox-sensitive E2 Rad6 controls cellular response to oxidative stress via K63-linked ubiquitination of ribosomes.

Journal Article Cell Rep · May 24, 2022 Protein ubiquitination is an essential process that rapidly regulates protein synthesis, function, and fate in dynamic environments. Within its non-proteolytic functions, we showed that K63-linked polyubiquitinated conjugates heavily accumulate in yeast ce ... Full text Link to item Cite

Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response

Journal Article Journal of Biological Chemistry · September 2021 Full text Cite

Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress.

Journal Article Proc Natl Acad Sci U S A · September 8, 2020 Subpopulations of ribosomes are responsible for fine tuning the control of protein synthesis in dynamic environments. K63 ubiquitination of ribosomes has emerged as a new posttranslational modification that regulates protein synthesis during cellular respo ... Full text Link to item Cite

Isoleucine 44 Hydrophobic Patch Controls Toxicity of Unanchored, Linear Ubiquitin Chains through NF-κB Signaling.

Journal Article Cells · June 2020 Ubiquitination is a post-translational modification that regulates cellular processes by altering the interactions of proteins to which ubiquitin, a small protein adduct, is conjugated. Ubiquitination yields various products, including mono- and poly-ubiqu ... Full text Cite

Expanding Role of Ubiquitin in Translational Control

Journal Article International Journal of Molecular Sciences · February 9, 2020 The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regu ... Full text Cite

Polyubiquitin Chains Linked by Lysine Residue 48 (K48) Selectively Target Oxidized Proteins In Vivo.

Journal Article Antioxidants & redox signaling · November 2019 Aims: Ubiquitin is a highly conserved protein modifier that heavily accumulates during the oxidative stress response. Here, we investigated the role of the ubiquitination system, particularly at the linkage level, in the degradation of oxidiz ... Full text Cite

Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress.

Journal Article Journal of proteome research · January 2019 During oxidative stress, K63-linked polyubiquitin chains modify a variety of proteins including ribosomes. Knowledge of the precise sites of K63 ubiquitin is key to understand its function during the response to stress. To identify the sites of K63 ubiquit ... Full text Cite

Phenazines Regulate Nap-Dependent Denitrification in Pseudomonas aeruginosa Biofilms

Journal Article Journal of Bacteriology · May 2018 ABSTRACTMicrobes in biofilms face the challenge of substrate limitation. In particular, oxygen often becomes limited for cells inPseudomonas aeruginosabi ... Full text Cite

Quantifying gene expression: the importance of being subtle

Journal Article Molecular Systems Biology · October 2016 Full text Cite

A synopsis on aging—Theories, mechanisms and future prospects

Journal Article Ageing Research Reviews · August 2016 Full text Cite

Recurrent Mutations of Chromatin-Remodeling Genes and Kinase Receptors in Pheochromocytomas and Paragangliomas

Journal Article Clinical Cancer Research · May 1, 2016 AbstractPurpose: Pheochromocytomas and paragangliomas (PPGL) are genetically heterogeneous tumors of neural crest origin, but the molecular basis of most PPGLs is unknown.Exp ... Full text Cite

Identification and quantification of K63-ubiquitinated proteins in neuronal cells by high-resolution mass spectrometry

Chapter · 2016 "This volume highlights proteomics studies of quantitative PTM changes in both peripheral and central nervous system proteomes utilizing the most recent advances in mass spectrometry. ... Full text Cite

K63 polyubiquitination is a new modulator of the oxidative stress response.

Journal Article Nature structural & molecular biology · February 2015 Ubiquitination is a post-translational modification that signals multiple processes, including protein degradation, trafficking and DNA repair. Polyubiquitin accumulates globally during the oxidative stress response, and this has been mainly attributed to ... Full text Cite

Redox Control of 20S Proteasome Gating

Journal Article Antioxidants & Redox Signaling · June 2012 Full text Cite

Protein Expression Regulation under Oxidative Stress

Journal Article Molecular & Cellular Proteomics · December 2011 Full text Cite

Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl‐based redox modification of the 20S proteasome

Journal Article The FEBS Journal · June 2008 The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys‐SH) into cysteine sulfenic acid (Cys‐SOH), followed by S‐glutathionylation (Cys‐S‐SG). Proteasome S‐glutathionylation promotes part ... Full text Cite

Reactive cysteine in proteins: Protein folding, antioxidant defense, redox signaling and more

Journal Article Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · July 2007 Full text Cite

Crystallization and preliminary X-ray crystallographic studies of glutaredoxin 2 from Saccharomyces cerevisiae in different oxidation states.

Journal Article Acta crystallographica. Section F, Structural biology and crystallization communications · April 2005 Glutaredoxins are small (9-12 kDa) heat-stable proteins that are highly conserved throughout evolution; the glutaredoxin active site (Cys-Pro-Tyr-Cys) is conserved in most species. Five glutaredoxin genes have been identified in Saccharomyces cerevisiae; h ... Full text Cite