Recent publications

Čabart, P. and Luse, D.S. (2012) Inactivated RNA polymerase II open complexes can be reactivated with TFIIE. J. Biol. Chem. 287, in press. [PubMed – in process; PMC to be supplied by publisher.]

Čabart, P., Újvári, A., Pal, M. and Luse, D.S. (2011) Transcription factor TFIIF is not required for initiation by RNA polymerase II but it is essential to stabilize transcription factor TFIIB in early elongation complexes. Proc. Nat. Acad. Sci. USA 108, 15786-15791. PMCID: PMC3179120 [Available on 2012/3/20]

Luse, D.S. and Studitsky, V.M. (2011) The mechanism of nucleosome traversal by RNA polymerase II: roles for template uncoiling and transcript elongation factors. RNA Biology 8, in press.

Újvári, A., Pal, M.  and Luse, D.S. (2011) The functions of TFIIF during initiation and transcript elongation are differentially affected by phosphorylation by casein kinase 2. J. Biol. Chem. 286, 23160-23167. PMCID: PMC3123083 [Available on 2012/7/1].

Luse, D.S., Spangler, L. and Újvári, A.  (2011) Efficient and rapid nucleosome traversal by RNA polymerase II depends on a combination of transcript elongation factors.  J. Biol. Chem. 286, 6040-6048. PMCID: PMC3057798 [Available on 2012/2/25].

Hsieh, F.-K., Fisher, M., Újvári, A., Studitsky, V.M. and Luse, D.S. (2010) Histone Sin mutations promote nucleosome traversal and histone displacement by RNA polymerase II. EMBO Reports 11, 705-710. PMCID: PMC2933865 [Available on 2011/9/1].

Újvári, A., Hsieh, F.-K., Luse, S.W., Studitsky, V.M. and Luse, D.S. (2008) Histone N-terminal tails interfere with nucleosome traversal by RNA polymerase II. J. Biol. Chem. 283, 32236-32243. PMCID: PMC2583294.

Bondarenko, V.A., Steele, L.M., Újvári, A., Gaykalova, D.A., Kulaeva, O.I., Polykanov, Y.S., Luse, D.S. and Studitsky, V.M. (2006) Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II. Mol. Cell 24, 469-479.

Újvári, A. and Luse, D.S. (2006) RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit. Nature Struct. Mol. Biol. 13, 49-54.

Pal, M., Ponticelli, A.S. and Luse, D.S. (2005) The role of the transcription bubble and TFIIB in promoter clearance by RNA polymerase II. Mol Cell 19, 101-110.

Újvári, A. and Luse, D.S. (2004) Newly initiated RNA encounters a factor involved in splicing immediately upon emerging from within RNA polymerase II. J. Biol. Chem. 279, 49773-49779.

Hawryluk, P., Újvári, A. and Luse, D.S. (2004) Characterization of a novel RNA polymerase II arrest site which lacks a weak 3' RNA-DNA hybrid. Nucleic Acids Res. 32, 1904-1916.

Pal, M. and Luse, D.S. (2003) The initiation-elongation transition: lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23. Proc. Natl. Acad. Sci. USA 100, 5700-5705.

Újvári, A., Pal, M. and Luse, D.S. (2002) RNA polymerase II transcription complexes may become arrested if the nascent RNA is shortened to less than 50 nucleotides. J. Biol. Chem. 277, 32527-32537.

Pal, M. and Luse, D.S. (2002) Strong natural pausing by RNA polymerase II within 10 bases of transcription start may result in repeated slippage and re-extension of the nascent RNA. Mol. Cell. Biol. 22, 30-40.

Pal, M., McKean, D. and Luse, D.S. (2001) Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence. Mol. Cell. Biol. 21, 5815-5825.

Keene , R.G. and Luse, D.S. (1999) Initially transcribed sequences strongly affect the extent of abortive initiation by RNA polymerase II. J. Biol. Chem. 274, 11526-11534.

Samkurashvili, I. and Luse, D.S. (1998) Structural changes in the RNA polymerase II transcription complex during the transition from initiation to elongation. Mol. Cell. Biol. 18, 5343-5354.

Orphanides, G., LeRoy, G., Chang, C.-H., Luse, D.S. and Reinberg, D. (1998) FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92, 105-116.

Chang, C.-H. and Luse, D.S. (1997) H3/H4 tetramers are sufficient to block transcript elongation by RNA polymerase II in vitro. J. Biol. Chem. 272, 23427-23434.