Stephen Lodmell

J. Stephen Lodmell
Adjunct Associate Professor

Email: stephen.lodmell@umontana.edu

Phone: (406) 243-6393

Steve Lodmell completed his Ph.D. research on the biochemistry and structural dynamics of the ribosome with Dr. Albert Dahlberg at Brown University in 1996. He then focused on the structure and biochemistry of HIV-1 genomic RNA during his postdoctoral research in the laboratory of Drs. Bernard and Chantal Ehresmann and Dr. Roland Marquet at the Université Louis Pasteur in Strasbourg France from 1996-1999. He arrived at UM in 1999 and maintains research projects on HIV RNA and on the structure and dynamics of ribosomes. Dr. Lodmell teaches undergraduate courses in Biochemistry and graduate courses in Nucleic Acids.

 

Research Interests

My research interests lie in the mechanisms of molecular recognition between biological macromolecules. In particular, I am interested in RNA-RNA and RNA-protein interactions in two different systems: those that are essential for specific replicative functions in retroviruses, and those that are important for ribosome function. The genomic RNA of HIV-2 contains not only coding information for proteins, but also functional signals for transactivation, dimerization, encapsidation, splicing, and poly A addition. Thus one major effort in my laboratory is to construct detailed secondary and tertiary structure maps of HIV-2 RNA functional motifs using solution structure probing techniques. The ultimate goal of this line of research is to understand the structure and functions of this crucial portion of the HIV genome in sufficient detail to be able to target it for antiretroviral chemotherapies. The other major thrust in our laboratory is using RNA chemical structure probing agents to investigate structural dynamics of the ribosome during protein synthesis. The high resolution crystal structures of the ribosome has recently been published which has given us a good look at the static structure of these universal subcellular particles. However, we know that the ribosome is quite dynamic during the processive catalysis of peptide bond formation, thus our efforts are focused on elucidating the important conformational changes that occur in the ribosome during protein synthesis.

Representative Publications

J.M. Lanchy, J.D. Ivanovitch, J.S. Lodmell (2003) A structural linkage between dimerization and encapsidation signals in HIV-2 RNA in vitro. RNA 9(8): 1007-1018.

S. Marzi, W. Knight, L. Brandi, E. Caserta, N. Soboleva, W.E. Hill, C.O. Gualerzi, and J.S. Lodmell (2003) Ribosomal localization of translation initiation factor IF2. RNA 9(8): 958-969.

J.-M. Lanchy, C.A. Rentz, J.D. Ivanovitch, and J.S. Lodmell. (2003) Elements located upstream and downstream of the major splice donor site influence the ability of HIV-2 leader RNA to dimerize in vitro. Biochemistry: 2634-2642.

E. L. Deer, B. Douk, J.-M. Lanchy, and J.S. Lodmell. (2003) Elucidation and characterization of oligonucleotide-accessible sites on HIV-2 leader region RNA. Antisense and Nucleic Acid Drug Development 13: 45-55.

J.S.Lodmell & S.P. Hennelly (2003). “Conformational Dynamics Within the Ribosome.” In Translational Mechanisms (Brakier-Gingras, L. & Lapointe, J., eds.). Landes Bioscience, Austin, TX.

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