RNA polymerase structure

Chapter 6 - The mechanism of transcription in bacteria. In this chapter we will focus on the basic mechanism of transcription. We will begin with RNA polymerase, the enzyme that catalyzes transcription. We will also look at the interaction between RNA polymerase and DNA.

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The main contents of this chapter include all of the following: Categories of activators, structures of the DNA-Binding motifs of activators, independence of the domains of activators, functions of activators, interaction among activators, regulation of transcription factors.

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The transcription patterns of 64 linear double stranded DNA templates obtained with T7 RNA polymerase were investigated. These templates consisted of 17 nucleotide-long sequences under the control of the minimal bac-teriophage T7 promoter and represented all possible combinations of nucleotides at positions +8, +10 and +11.

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RNA polymerase II (pol II) produces all mRNA in eukaryotic cells. Structures of the ten-subunit core of yeast pol II in free form [1, 2], in complex with DNA and RNA [3], and in complex with alpha-amanitin [4] have elucidated the mRNA transcription mech-anism [reviewed in 5, 6]. Based on this work, models for the com-plete 12-subunit pol II were obtained [7, 8]. We have subsequently solved the first structure of pol II in complex with a transcription factor, the elongation factor TFIIS [9, 10].

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The bacterial Lsm protein, host factor I (Hfq), is an RNA chaperone involved in many types of RNA transactions such as replication and stabil-ity, control of small RNA activity and polyadenylation. In this latter case, Hfq stimulates poly(A) synthesis and binds poly(A) tails that it protects from exonucleolytic degradation. We show here, that there is a correlation between Hfq binding to the 3¢ end of an RNA molecule and its ability to stimulate RNA elongation catalyzed by poly(A)polymerase I.

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BacterialRNApolymerase (RNAP) is the central enzyme of gene expression that is responsible for the synthesis of all types of cellular RNAs. The process of transcription is accompanied by complex structural rearrangements of RNAP. Despite the recent progress in structural studies of RNAP, detailed mechanisms of conformational changes of RNAP that occur at different stages of transcription remain unknown.

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GE23077, a novel microbial metabolite recently isolated from Actinomadurasp. culture media, is a potent and selective inhibitor of bacterial RNApolymerase (RNAP). It inhibitsGram-positive (Bacillus subtilis) andGram-negative (Escherichia coli)RNAPs with IC50 values (i.e. the concen-tration at which the enzyme activity is inhibited by 50%) in the 10 )8 Mrange, whereas it is not active onE. coliDNA polymerase or on eukaryotic (wheat germ) RNAP II (IC50 values10 )4 Min both cases).

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In the first half of the talk, the current state of our ongoing structure-function analysis of the mRNA transcription cycle will be dis-cussed. The crystallographic structures of the complete 12-subunit RNA polymerase II in free form and with bound DNA and RNA have been determined as atomic models. The structure of the complete Pol II elongation complex bound by the transcript cleavage factor TFIIS explained how Pol II uses a single tunable active site for both RNA synthesis and RNA cleavage.

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Symposia Lectures Monday Monday, July 9, 2007 A2-L1 J. Diffley No abstract available. A2-L2 Molecular bioimaging of gene transcription P. Cramer Gene Center, Munich, GERMANY In the first half of the talk, the current state of our ongoing structure-function analysis of the mRNA transcription cycle will be discussed. The crystallographic structures of the complete 12-subunit RNA polymerase II in free form and with bound DNA and RNA have been determined as atomic models.

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SurE, the stationary-phase survival protein of Salmonella typhimurium, forms part of a stress survival operon regulated by the stationary-phase RNA polymerase alternative sigma factor. SurE is known to improve bacterial viability during stress conditions.

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With the use of photoresponsive T7 promoters tethering two 2¢-methylazo-benzenes or 2¢,6¢-dimethylazobenzenes, highly efficient photoregulation of DNA transcription was obtained. After UV-A light irradiation (320–400 nm), the rate of transcription with T7 RNA polymerase and a photoresponsive promoter involving two 2¢,6¢-dimethylazobenzenes was 10-fold faster than that after visible light irradiation (400–600 nm).

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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Avian reovirus L2 genome segment sequences and predicted structure/function of the encoded RNA-dependent RNA polymerase protein

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