Cell Biology

Faculty and Research Interests

Michael Anikin, PhD

Assistant Professor
Science Center 230 (Lab)
Science Center B207 (Lab)
856-566-6326
anikinmi@umdnj.edu

Education

Moscow State Academy of Fine Chemical Technology,
PhD, 1988.

 

Research Interests

Research in the laboratory focuses on mechanisms of transcription as the first stage of gene expression. We study structure-function relationships in the central enzyme involved in transcription, DNA-dependent RNA polymerase. Our model transcription system is based on the single-subunit RNA polymerase from yeast mitochondria. We assemble active transcription complexes using highly-purified recombinant protein components and synthetic oligonucleotides and employ a combination of biochemical and genetic techniques to elucidate the structural elements of the enzyme that are functionally important during early steps of promoter recognition, transcription initiation and elongation.

Recent Publications

1. Bandwar RP, Ma N, Emanuel SA, Anikin M, Vassylyev DG, Patel SS, McAllister WT. The transition to an elongation complex by T7 RNA polymerase is a multistep process. J Biol Chem. 2007 Aug 3;282(31):22879-86.
2. Kashkina E, Anikin M, Brueckner F, Lehmann E, Kochetkov SN, McAllister WT, Cramer P, Temiakov D. Multisubunit RNA polymerases melt only a single DNA base pair downstream of the active site.  J Biol Chem 2007, May 24; 282(30):21578-82.
3. Pomerantz RT, Temiakov D, Anikin M, Vassylyev DG, McAllister WT.  A mechanism of nucleotide misincorporation during transcription due to template-strand misalignment.  Mol Cell. 2006 Oct 20; 24(2):245-55.
4. Kashkina E, Anikin M, Brueckner F, Pomerantz RT, McAllister WT, Cramer P, Temiakov D.  Template misalignment in multisubunit RNA polymerases and transcription fidelity. Mol Cell. 2006 Oct 20; 24(2):257-66.
5. Kashkina E, Anikin M, Tahirov TH, Kochetkov SN, Vassylyev DG, Temiakov D.  Elongation complexes of Thermus thermophilus RNA polymerase that possess distinct translocation conformations. Nucleic Acids Res. 2006; 34(14):4036-45.
6. K. Ma, D. Temiakov, M. Anikin, W.T. McAllister.  Probing conformational changes in T7 RNA polymerase during initiation and termination by using engineered disulfide linkages.  Proc Natl Acad Sci USA 102, No 49, 17612-7 (2005).
7. R.T. Pomerantz, R. Ramjit, Z. Gueroui, C. Place, M. Anikin, S. Leuba, J. Zlatanova, W.T. McAllister.  A tightly regulated molecular motor based upon T7 RNA polymerase.  Nano Letters 5, No 9, 1698-703 (2005).
8. D. Temiakov, V. Patlan, M. Anikin, W.T. McAllister, S. Yokoyama, D.G. Vassylyev.  Structural basis for substrate selection by T7 RNA polymerase.  Cell 116, No 3, 381-91 (2004)
9. D. Temiakov, M. Anikin, K. Ma, M. Jiang, W.T. McAllister.  Probing the organization of transcription complexes using photoreactive 4-thio-substituted analogs of uracil and thymidine.  Methods Enzymol. 371, 133-43 (2003)
10. D. Temiakov, T. Tahirov, M. Anikin, W.T. McAllister, D.G. Vassylyev, S. Yokoyama.  Crystallization and preliminary crystallographic analysis of T7 RNA polymerase elongation complex.  Acta Crystallogr D Biol Crystallogr. 59 (Pt 1), 185-7 (2003)
11. T.H. Tahirov, D. Temiakov, M. Anikin, V. Patlan, W.T. McAllister, D.G.Vassylyev, S.Yokoyama.  Structure of a T7 RNA polymerase elongation complex at 2.9 A resolution. Nature 420, No 6911, 43-50 (2002)
12. D. Temiakov, M. Anikin, W.T. McAllister.  Characterization of T7 RNA polymerase transcription complexes assembled on nucleic acid scaffolds.  J. Biol. Chem. 277  (2002)
13. K. Ma, D. Temiakov, M. Jiang, M. Anikin, W.T. McAllister.  Major conformational changes occur during the transition from an initiation complex to an elongation complex by T7 RNA polymerase. J. Biol. Chem. 277, No 45, 43206-15 (2002).
14. D. Imburgio, M. Anikin, W.T. McAllister.  Effects of substitutions in a conserved DX2GR sequence motif, found in many DNA-dependent nucleotide polymerases, on transcription by T7 RNA polymerase. J Mol Biol. 319, No 1, 37-51 (2002)