a 2009

Backbone dynamics of N-terminal Domain of the Delta Subunit of Bacterial RNA Polymerase

KADEŘÁVEK, Pavel, Carl DIEHL, Veronika MOTÁČKOVÁ, Lukáš ŽÍDEK, Libor KRÁSNÝ et. al.

Basic information

Original name

Backbone dynamics of N-terminal Domain of the Delta Subunit of Bacterial RNA Polymerase

Authors

KADEŘÁVEK, Pavel, Carl DIEHL, Veronika MOTÁČKOVÁ, Lukáš ŽÍDEK, Libor KRÁSNÝ and Mikael AKKE

Edition

Structural Biology Network 13th Annual Conference, 2009

Other information

Type of outcome

Konferenční abstrakt

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Organization unit

Faculty of Science
Změněno: 3/7/2010 19:04, Mgr. Pavel Kadeřávek, Ph.D.

Abstract

V originále

The RNA polymerase consists of eight subunits. A dimer of two alpha subunits holds together two beta subunits which form the active site. The sigma subunit is responsible for both promoter recognition and ranscription initiation [1], whereas the roles of the two omega subunits are poorly understood. The delta subunit increases both the transcriptional specificity [2],[3],[4],[5],[6],[7] and the efficiency of RNA synthesis [5],[6],[7]. The delta subunit and one of the omega subunits are not conserved throughout all bacterial species. Here we present the backbone dynamics of the N-terminal domain of the delta subunit of bacterial RNA polymerase from Bacillus subtilis. The N-terminal domain of the delta subunit has a well-defined structure, while the C-terminal domain is unstructured and highly negatively charged. Here we focus on the isolated N-terminal domain, whose structure consists of an alpha helical core and a short beta sheet [8]. The standard set of 15-N relaxation experiments (R1,R2,NOE) were performed at two magnetic field (500MHz, 600MHz) in order to analyze fast ns-ps backbone motions. The relaxation experiments were acquired at two temperatures (300K, 280K) in order to get a more comprehensive description. Slow motions on the ms-us timescale were investigated by CPMG and T1rho relaxation dispersion experiments. An interesting dynamic behavior was revealed in the region involving the short beta sheet and its proximity. REFERENCES: [1] Cramer P., Current Opinion in Structural Biology, 12, 89-97, 2002 [2] Achberger E.C., Whiteley H.R., Journal of Biological Chemistry, 256, 7424-7432, 1981 [3] Achberger E.C., Tahara M., Whiteley H.R., Journal of Bacteriology, 150, 977-980, 1982 [4] Dobinson K.F., Spiegelman G.B., Biochemistry, 26, 8206-8213, 1987 [5] Juang Y.L., Helmann J.D., Journal of Molecular Biology, 239, 1-14, 1994 [6] Juang Y.L., Helmann J.D., Biochemistry, 34, 14270-14270, 1995 [7] Juang Y.L., Helmann J.D., Biochemistry, 34, 8465-8473, 1995 [8] Motáčková V., Šanderová H., Nováček J., Žídek L.,Sklenář V., Krasný L., (poster), 7th Discussions in Structural Molecular Biology, Nové Hrady, 2009