Jared Schrader

Jared Schrader

Research interest(s)/area of expertise

• Molecular systems biology

• mRNA translation and decay

• Genome-wide high-throughput methods in bacteria

• Host-pathogen interactions

• Chemical biology

Research

Sub-cellular organization of mRNA decay in bacteria

In eukaryotic cells, mRNA decay is often organized in ribonucleoprotein granules like RNA processing-bodies or stress granules. We found that bacteria can also make similar ribonucleoprotein granules that we termed bacterial ribonucleoprotein bodies (BR-bodies) composed of Ribonuclease E, protein components of the RNA degradosome, and RNA. These BR-bodies appear to be important for mRNA degradation and are assembled by liquid-liquid phase separation from the cytoplasm forming a compartment with high concentrations of the RNA degradosome and RNA. Here were's currently utilizing high-throughput mRNA decay assays and cell biology experiments to probe the role of these granules in mRNA decay.

Role of BR-bodies in host colonization

BR-bodies promote rapid mRNA decay which allows bacteria to quickly adapt their transcriptomes to their changing environments.  We are investigation how BR-bodies impact host colonization, as Tn-insertion mutants in various species have shown a reduction in fitness during host colonization.  We are currently characterizing which species BR-bodies play a role in host colonization, and also by which molecular mechanisms they use to promote host colonization.

Mechanisms of non-Shine-Dalgarno translation initiation

The mechanism of translation initiation in bacteria was first examined in E. coli, where the presence of a Shine-Dalgarno site preceding the start codon leads to the initiation of translation in the proper reading frame. Now with thousands of sequenced bacterial genomes it was discovered that less than 1/2 of all bacterial protein coding genes are preceded by a Shine-Dalgarno site. Additionally, individual bacterial species including many cyanobacteria and bacteroidetes, lack Shine-Dalgarno sites in nearly 90% of their genes! We are therefore investigating the mechanisms of non-Shine-Dalgarno initiation by utilizing Caulobacter crescentus. Caulobacter contains Shine-Dalgarno sites in only 23.5% of its genes, has a doubling time of less than two hours, has well established genetic tools, and has a well annotated transcriptome. We are currently utilizing ribosome profiling, translation reporters, and in vitro reconstituted translation initiation assays to dissect the factors required for non-Shine-Dalgarno initiation.

Education

• Postdoctoral Fellowship, Stanford University, 2011-2015
• Ph.D. in Biophysical Chemistry, Northwestern University, 2011
• B.S. in Microbiology, Colorado State University, 2005

Awards and grants

• WSU Career Chair Award, 2023

• Junior Faculty Award, WSU Academy of Scholars, 2018

• NIH NIGMS MIRA Award R35GM124733, 2017-2027

Selected publications

• Nandana V, Rathnayaka-Mudiyanselage IW, Muthunayake NS, Hatami A, Mousseau CB, Ortiz-Rodríguez LA, Vaishnav J, Collins M, Gega A, Mallikaarachchi KS, Yassine H, Ghosh A, Biteen JS, Zhu Y, Champion MM, Childers WS, Schrader JM. The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions. Cell Rep. 2023
• Al-Husini, N., D. T. Tomares, Z. Pfaffenberger, N. S. Muthunayake, M. A. Samad, T. Zuo, O. Bitar, J. R. Aretakis, M.-H. M. Bharmal, A. Gega, J. S. Biteen, W. S. Childers and J. M. Schrader. BR-bodies provide selectively permeable condensates that stimulate mRNA decay and prevent release of decay intermediates. Molecular Cell 2020
• Al-Husini, N., Tomares, D.T., Bitar, O., Childers, W.S., Schrader, J.M. α-proteobacterial RNA degradosomes assemble liquid-liquid phase separated RNP bodies. Molecular Cell, 2018

Other qualifications directly relevant to courses taught

• Board Member – Michigan Branch of the American Society of Microbiology
• Member of the WSU Institutional Biosafety Committee

Citation index

• Google Scholar

Courses taught by Jared Schrader

Winter Term 2025 (future)

• BIO3100 - Cellular Biochemistry

Fall Term 2024 (current)

• BIO6510 - Molecular Interactions
• BIO7520 - Nucleic Acid Laboratory
• MGG7015 - Introduction to Genetics

Fall Term 2023

• MGG7015 - Introduction to Genetics

Winter Term 2023

• BIO6530 - Protein Structure and Dynamics
• BIO7530 - Proteins Laboratory

Fall Term 2022

• BIO6510 - Molecular Interactions
• BIO7520 - Nucleic Acid Laboratory
• MGG7015 - Introduction to Genetics

Winter Term 2022

• BIO3100 - Cellular Biochemistry
• PHC8888 - Survey of Research at the Chemistry Biology Interface