Journal Browser

Journal Browser

Special Issue "RNA Polymerases as Molecular Machines"

A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: closed (20 September 2013).

Special Issue Editor

Dr. Jianhua Fu
Guest Editor
Department of Biochemistry, Medical College of Wisconsin, 303 Basic Science Bldg., Milwaukee, WI 53226, USA
Interests: RNA polymerase II; gene transcription and regulation in eukaryotic cells

Special Issue Information

Dear Colleagues,

Transcription is the first step of gene expression, which is catalyzed by RNA polymerases through three sequential stages: transcription initiation, elongation and termination. Although cellular RNA polymerases carry at the core of their structures only the plain activity that catalyzes successively formation of phosphodiester bonds, a network of proteins and protein-ribonucleic acid complexes impinge on the polymerases and impart high-order functions of great complexity. These regulatory factors are able to interact with a cognate RNA polymerase to form high-order structures each responsible for a specific stage or step through the transcription cycle. It is a wonder how massive and complicated these structures can be and how precisely specific their functions are defined. For instance, RNA polymerase II (Pol II, 12-subunit with M.W. of 513 KDa) assembles with five general (or basal) transcription factors onto core regions of Pol II-specific promoters to form the pre-initiation complex (PIC, 31-subunit with M.W. > 1 MDa) with a precise biochemical and structural definition. The Pol II structure then varies as driven by the ATP hydrolysis and initial phosphodiester-bond formation during transcription initiation, and escapes into the early elongation complex in which elongation factors are bound while the initiation factors have dissociated. Factor exchange and conformation remodeling events also occur once Pol II has read polyadenylation and termination sequences and cause the polymerase to disengage from a template DNA. As such, RNA polymerase systems have been viewed as protein machines equipped with molecular devices capable of tuning the activities with great intricacy. In eukaryotic systems, yet additional complexity and layers of regulation are attained from the organization of genomic DNA. Nuclear DNAs wrap around the heteromeric histone octomer to assemble the compact nucleosome core particle, and with the aid of linker histone, nucleosomes further organize into high-order chromatin structures that are much more compact and resistant to transcription. To large degrees, the interplay between RNA polymerase machineries and chromatin structures is what determines the activity state of a eukaryotic genome. Biochemical and structural studies over the past two decades have uncovered many details about the structure-and-function relationships that regulate cellular RNA polymerase machines. Take again the Pol II machinery for instance, the PIC is regulated within the much larger holo-Pol II complex that also includes the Mediator complex, and the conformation of Mediator appears to shift according to what DNA sequence-specific activator is involved, thus generating gene-specificity. Pol II molecules that escape from the promoter-centered PIC then become subject to actions from elongation factors which can be either stimulatory or inhibitory, and also responsive to signaling pathways. The transition from initiation at the promoter to early elongation proximal to the promoter is a major window of regulation for especially responsive genes such as those involved in cell development. Throughout the early-elongation and next phase, which is the productive elongation of RNA chain, the polymerase directly and indirectly interacts with yet other diverse proteins, and the new Pol II complexes thus formed obligate active transcriptions to RNA processing (e.g. 5’ capping and splicing) events and chromatin-modifying activities (e.g. histone methylation). Finally as Pol II approaches the 3’-end of an open-reading frame, it recruits the 3’ processing and polyadenylation machinery onto the elongation complex to induce transcript cleavage, addition of an adenosine string to RNA 3’ end, and termination of transcription. Pol II molecules that have disengaged from DNA templates rapidly receive a posttranslational modification that returns the polymerases to the state suitable for another round of initiation. The control of polymerase activities throughout these stages of the transcription cycle requires temporal and spatial coordination among the diverse groups of factors involved in the machinery. A large part of the current research effort in the field is directed at elucidating the biochemical and structural details that underlie the processes. The purpose of this special issue of Molecules is to highlight mechanistic understandings gained from recent studies of various RNA polymerase machineries, with a particular viewpoint of structure-and-function relationship.

Dr. Jianhua Fu
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • RNA polymerase
  • transcription initiation
  • transcription elongation
  • transcription fidelity
  • RNA polymerase translocation
  • RNA polymerase structure
  • CTD phosphorylation
  • CTD dephosphorylation
  • Mediator complex
  • transcript processing
  • transcription termination

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:


Open AccessReview
Cross-Talk of Phosphorylation and Prolyl Isomerization of the C-terminal Domain of RNA Polymerase II
Molecules 2014, 19(2), 1481-1511; - 27 Jan 2014
Cited by 7
Post-translational modifications of the heptad repeat sequences in the C-terminal domain (CTD) of RNA polymerase II (Pol II) are well recognized for their roles in coordinating transcription with other nuclear processes that impinge upon transcription by the Pol II machinery; and this is [...] Read more.
Post-translational modifications of the heptad repeat sequences in the C-terminal domain (CTD) of RNA polymerase II (Pol II) are well recognized for their roles in coordinating transcription with other nuclear processes that impinge upon transcription by the Pol II machinery; and this is primarily achieved through CTD interactions with the various nuclear factors. The identification of novel modifications on new regulatory sites of the CTD suggests that, instead of an independent action for all modifications on CTD, a combinatorial effect is in operation. In this review we focus on two well-characterized modifications of the CTD, namely serine phosphorylation and prolyl isomerization, and discuss the complex interplay between the enzymes modifying their respective regulatory sites. We summarize the current understanding of how the prolyl isomerization state of the CTD dictates the specificity of writers (CTD kinases), erasers (CTD phosphatases) and readers (CTD binding proteins) and how that correlates to transcription status. Subtle changes in prolyl isomerization states cannot be detected at the primary sequence level, we describe the methods that have been utilized to investigate this mode of regulation. Finally, a general model of how prolyl isomerization regulates the phosphorylation state of CTD, and therefore transcription-coupled processes, is proposed. Full article
(This article belongs to the Special Issue RNA Polymerases as Molecular Machines)
Show Figures

Figure 1

Back to TopTop