December 20, 2015

About 6 years ago, Dartmouth secured an INBRE award - this is an NIH grant that pairs faculty at research universities with small colleges in the same state.  I participate in the New Hampshire (NH)-INBRE program - check out their web page here.  I work with Lori Bergeron at New England College (pictured here).  Our original project focused on studying iron metabolism in the oral microbe Actinomyces oris.  This project involves undergraduates working at NEC and NEC students visiting my lab for the summer. This work was recently published. More recently, Lori has focused her efforts on the study of c-di-GMP synthesis in the soil microbe Pseudomonas fluorescens, working closely with members of my group.  The NH-INBRE program presents a terrific opportunity to expose students at smaller schools to cutting edge research at top universities.

December 17, 2015

The Journal of Bacteriology is 100 years old in 2016!  Here is a link to the first article in the journal by W.T. Sedgewick, "THE GENESIS OF A NEW SCIENCE,-BACTERIOLOGY" -- this article is a wonderful history of microbiology as of 1916, and argues strongly for the birth of a new journal to cover a new discipline.  It is really inspiring!  The cover of the first issue is shown on the left (thanks to Jeff Karr at the ASM Archives!)

As part of the celebration of the journal's impact on microbiology over the past 100 year, keep an eye out for "Classic Spotlights" - short 1-2 paragraph overviews of articles in JB and how those articles impacted the field of microbiology.  I was fortunate to be able to contribute a Classic Spotlight in an early issue of 2016.  This article entitled "Before They Were Biofilms" talks about some of the seminal papers describing microbial attachment to surfaces.  I often think of these papers when considering about our own data - and these studies in JB still inspire me today.

December 15, 2015

One important question we have been studying relates to the role of c-di-GMP signaling during biofilm formation.  Pseudomonas fluorescens has 50+ proteins that make, break or bind c-di-GMP.  How does the organism coordinate the action of all of these proteins to specify a particular output?  Kurt Dahlstrom, a PhD student in the lab, recently published a paper in mBio illustrating one mechanism which might drive this specificity.  He showed that an enzyme that makes c-di-GMP (the diguanylate cyclase GcbC) can interact with a c-di-GMP receptor protein (LapD) using bacterial two-hybrid and pull-down assays, and that this interaction is required for full signaling to occur.  Working with Krista Giglia and Holger Sondermann at Cornell, who solved the structure of GcbC, Kurt was able to use genetic students to identify surface helices on GcbC and LapD that drive this protein-protein interaction.  Furthermore, using the information from his studies of GcbC and LapD, he was able to engineer better interactions between LapD and a non-cognate diguanylate cyclase, and predict an interaction in Pseudomonas aeruginosa.  I feel that this work is an important advance in our understanding of  c-di-GMP signaling specificity in bacteria.  This work was supported by funds from the NSF and NIH.