Waksman Funded Projects

A list of currently funded research projects as reported by various funding sources.

Areas of Research

More than a few Model organisms at work: Maize, Drosophila, C. Elegans, Mice, Tobacco, Yeast, E.coli, Algae and more.

SpirodelaBase

Methods and Tools to aid researchers.

In the News: High School Student Makes Duckweed Discovery

Old Bridge Student Finds Unknown Gene in Duckweed During a Student Scholar Program at Rutgers University

High-throughput Sequencing Services Available from the Waksman Genomics Core Facility

Genomics Facility's High-Throughput, Next Generation Systems offers major advancements in throughput and maximum savings with new technology.

Located on Busch Campus of Rutgers, The State University of New Jersey, the Waksman Institute of Microbiology is an interdisciplinary research institute devoted to excellence in basic research. Focus areas include developmental biology, cell biology, biochemistry, structural biology, genetics, and genomics.

To support the educational mission of Rutgers, Waksman faculty members hold appointments in academic departments throughout the university. Our researchers train undergraduate students, graduate students, and post-doctoral fellows, as well as engage high school students in research through an outreach program.

Latest News

With generous support from Chancellor of Rutgers New Brunswick, we are pleased to announce the acquisition of a PacBio Sequel DNA sequencer. The Sequel uses Single Molecule Real Time (SMRT) technology to produce long reads, uniform coverage, and high consensus accuracy. The Sequel long 10-15kb reads are ideal for whole genome sequencing, full-length transcript sequencing, or sequencing of long amplicons. Additionally, its SMRT sequencing technology can also be used to directly detect DNA base modifications.

Rutgers Today Media Contact: Todd B. Bates

Ten Rutgers professors have been named fellows of the American Association for the Advancement of Science (AAAS), an honor conferred on 381 other experts in the U.S. and abroad.

The fellows were chosen by their AAAS peers for efforts to advance science applications that are deemed scientifically or socially distinguished, according to the AAAS.

By Deborah Walsh, Suburban Trends
Although some students might relish a respite from the most challenging of school work over the summer months, a couple of Kinnelon High School (KHS) students seized an opportunity to conduct high level scientific research at the Waksman Student Scholars Program (WSSP) Summer Institute at Rutgers University.
 

Madelaine Travaille, the school district's science supervisor, said a science research club was started at KHS in the 2015-16 school year.

Andrea Gallavotti, Assistant Professor in the Department of Plant Biology at the Waksman Institute, is a Co-PI of a recently awarded five-year collaborative grant. The project, sponsored by the National Science Foundation and titled “Genomic and Synthetic Approaches Linking Auxin Signaling Modules to Functional Domains in Maize”, seeks to understand how auxin signaling regulates the formation of specific functional domains in maize inflorescences (http://www.nsf.gov/awardsearch/showAward?AWD_ID=1546873).

 

Karl Maramorosch, 101, professor emeritus, Department of Entomology, School of Environmental and Biological Sciences, Rutgers University–New Brunswick, passed away of natural causes on May 9, 2016, during a visit to Poland.

Recent Publications

Zhang, W, Messing J.  In Press.  PacBio RS for gene family studies. Methods in Molecular Biology. Haplotyping.
Wu, Y, Messing J.  In Press.  Understanding and improving protein traits in maize seeds. Achieving Sustainable Maize Cultivation.
Lin, W, Mandal S, Degen D, Liu Y, Ebright YW, Li S, Feng Y, Zhang Y, Mandal S, Jiang Y et al..  2017.  Structural basis of Mycobacterium tuberculosis transcription and transcription inhibition.. Molecular Cell. 166:169-179. Abstract
Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis, which kills 1.8 million annually. Mtb RNA polymerase (RNAP) is the target of the first-line antituberculosis drug rifampin (Rif). We report crystal structures of Mtb RNAP, alone and in complex with Rif, at 3.8-4.4 Å resolution. The results identify an Mtb-specific structural module of Mtb RNAP and establish that Rif functions by a steric-occlusion mechanism that prevents extension of RNA. We also report non-Rif-related compounds-Nα-aroyl-N-aryl-phenylalaninamides (AAPs)-that potently and selectively inhibit Mtb RNAP and Mtb growth, and we report crystal structures of Mtb RNAP in complex with AAPs. AAPs bind to a different site on Mtb RNAP than Rif, exhibit no cross-resistance with Rif, function additively when co-administered with Rif, and suppress resistance emergence when co-administered with Rif.
Walker, SS, Degen D, Nickbarg E, Carr D, Soriano A, Mandal M B, Painter RE, Sheth PR, Xiao L, Sher X et al..  2017.  Affinity selection-mass spectrometry identifies a novel antibacterial RNA polymerase inhibitor.. ACS Chemical Biology. Abstract
The growing prevalence of drug-resistant Gram-negative bacteria is a significant global threat to human health. Rifampicin, an RNA polymerase-targeting agent, is an important part of the antibacterial armamentarium; however the emergence of resistance requires that it be used against only certain infections and usually in combination with another antibiotic. While rifampicin has significant clinical limitations, it does show that bacterial RNA polymerase can be an effective target for antibacterial intervention. To find new RNA polymerase inhibitors we initiated a screen of a collection of antibacterial bioactive molecules using affinity selection-mass spectrometry and purified Escherichia coli core RNA polymerase (subunits α, β, β', ω). Affinity selection screening identified a novel small molecule, MRL-436, that binds selectively to and inhibits RNA polymerase in vitro and inhibits RNA synthesis in the cell. Selection for resistance followed by whole genome sequencing identified a missense mutation in rpoC (β' subunit) and, separately, frameshift mutations in rpoZ (ω subunit) suggesting that MRL-436 targets RNA polymerase in the cell. In addition, cells lacking the rpoZ gene or purified RNA polymerase containing either a specific substitution in β' or lacking ω are selectively resistant to MRL-436. Molecular modeling indicates that the location of the substitution mutation in β' is closely juxtaposed with ω in a region of the complex thought to be important for transcription regulation during cellular response to amino acid starvation.