Postdoc:

Eric Gillitzer -I returned to Montana in November of 2001 to
join Mark Young's Lab. I did my undergraduate work at Montana State University, obtaining my  B.S. in Microbiology. I did my graduate work at Cold Spring Harbor Laboratory, working on protein-protein and protein-DNA interactions involved in replication complex formation. I switched gears when I came to Mark’s lab and I am now involved with the CCMV/nanotechnology project. I have been studying our ability to derivitize the surface of CCMV by a variety of methods and determining the location of those modifications.  I am examining the ability to label the surface of CCMV, dissassemble the particle and then reassemble the particle using differentially modified subunits in an attempt to generate chimeric protein cages. 

Another avenue of research I am exploring is the extent to which the protein cage needs to be either chemically or genetically modified for crosslinking in order to increase the range of pH and temperature the particle is stable over. This will hopefully allow us to mineralize the cage under conditions that will allow the formation of not only iron oxide in the form of rust in the interior of the cage, but allow the formation of other oxides such as magnatite and maghematite in the interior of the cage.

Some of my hobbies I enjoy outside of the laboratory are hunting, fishing, playing rugby and shooting. While I have been a fly fisherman for quite some time, I have begun to fish for walleye and other warm water species with some friends of mine on the local lakes. I have an interest in mechanics and spend time repairing/rebuilding my SAABs, my Isuzu Trooper and a 1965 Austin Healey Sprite.

For more information contact Eric
gillitzer@montana.edu

Graduate Students:

Blake Wiedenheft -My research has focused on the isolation and characterization of viruses found in the extreme thermal feature of Yellowstone National Park (YNP). These viruses and their hosts thrive in environments that are often nothing less then boiling pools of acid. The surprising discovery of life in these hostile environments has fueled my interests in understanding what is required for life at high temperatures. Viruses have become my primary tool for addressing these and other question concerning the microbial life present here. I have recently isolated and sequenced the genome of an SSV (Sulfolobus shibatae virus) virus from a thermal pool in the Norris Geyser Basin in YNP. This spindle shaped (60X90nm) virus is morphologically identical to other SSVs isolated from thermal features on other continents. I have used the Yellowstone isolate in a comparative genomic analysis with the other sequenced SSVs and have identified a subset of open reading frames (ORFs) that are common among all sequenced isolates. We speculate that the potential proteins encoded on these ORFs may represent common viral functions, a common evolutionary history and may represent the minimal replicon for this viral family.
My work with the SSV viruses has required me to become familiar with the archaeal host, Sulfolobus. Sulfolobus species are thermophilic acidophiles that grow optimally at 80C and pH 3. These high temperature acidic environments commonly contain toxic concentrations of iron (30mM). Therefore, Sulfolobus and other life in these environments must have efficient mechanisms for coping with iron toxicity. Ferritins are multimeric proteins that self-assemble into 9-13nm protein cages. These cages function to efficiently sequester iron and store it as a mineral core. I have isolated a ferritin like protein from S. solfataricus. This is the first example of a ferritin in the archaeal domain and its characterization will provide insights on iron metabolism in extreme environments. Additionally, the intrinsic mineralization properties of this thermal stable cage make it an attractive platform for applications in the field of nano-technology.
Future ambitions include, a survey of anaerobic life in these extreme environments, the employment of viruses in the investigation of archaeal transcriptional and translational processes and to develop the use of Sulfolobus ferittin in nano-technology.

For more information contact Blake
wiedenheft@montana.edu

George Rice:
grice@montana.edu

Jamie Snyder:
jsnyder@montana.edu

Undergraduates:
Josh Spuhler:
Sara Nichols:
Ben Widener:
Gwen Smith:
Heather Spuhler:
Loren Barber:

 

Technicians:

Sue Brumfield - I maintain and operate the transmission electron microscopy facility on campus under the direction of Mark Young. We have two electron microscopes available for general use, an older Zeiss 100CA equipped with a plate camera and a new LEO 912 with a 2K X 2K CCD camera. The new LEO 912 is equipped with the in-column OMEGA energy filtering system which allows us to do elastic and inelastic imaging including element localization (ESI) and electron energy loss spectra (EELS). It also is equipped with a cryo stage which we are currently using for virus reconstruction. Along with the electron microscopes, our lab has ancillary equipment needed for thin sectioning, shadow casting, and cryo work. I am also familiar with yeast fermentation technology and work with Pichia pastoris in a heterologous expression system used to produce CCMV protein cages.

For more information contact Sue
uplsb@montana.edu

Debbie Willits -
dwillits@montana.edu

Collaborators:

Dr. Trevor Douglas
Dept of Chemistry & Biochemistry
Gaines Hall Room 122
994-6566
tdouglas@chemistry.montana.edu
http://www.chemistry.montana.edu/tdouglas.html

Douglas Lab Members:

Postdocs:
Michael Klem:
Maria Nesterova:

Graduate Students:

Mark Allen:

Michelle Flenniken:

Janet Mendonca:

Zach Varpness: I have been working with a specific mutant of a small heat shock protein,G41C, which has a cysteine on the inside of the protein cage. Using the reactivity of the cysteine, we have attached a DNAse enzyme mimic, 5-Iodoacetamido-1,10-phenanthroline copper. We have encapsulated the enzyme mimic in the protein cage to examine the reactivity of the enzyme mimic on the inside of the protein. We also have a small heat shock protein mutant with a cysteine on the outside that we are going to react with the same enzyme mimic to compare the reactivity between inside and outside of the protein.

Lars Liepold

Undergraduates:
Jesse Mosolf
Daniel Ensign
Raina Gough
Eric Smith
Bridgid Crowley
 

Dr. Mary Cloninger
Dept. of Chemistry & Biochemistry
Gaines Hall Room 119
994-3051
mcloninger@chemistry.montana.edu
http://www.chemistry.montana.edu/mcloninger.html
 

Dr. David Singel
Dept. of Chemistry & Biochemistry
Gaines Hall Room 227
994-3960
rchds@montana.edu
http://www.chemistry.montana.edu/singel.html

Dr. Yves Idzerda
Dept. of Physics
Engineering Physical Sciences Bldg Room 242
994-7838
idzerda@physics.montana.edu
http://www.physics.montana.edu/faculty/idzerda/idzerda.htm

Dr. John Peters
Dept. of Chemistry & Biochemistry
Leon Johnson Hall Room 614
994-7211
john.peters@chemistry.montana.edu

Dr. John Scilagyi
Dept. of Chemistry & Biochemistry
Gaines Hall  Room