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Structure of Wild Type Yeast RNA Polymerase II and Location of RPB4 and RPB7

Published online by Cambridge University Press:  02 July 2020

Grant J. Jensen
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA94305
Gavin Meredith
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA94305
David A. Bushnell
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA94305
Roger D. Kornberg
Affiliation:
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA94305
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Extract

Nucleic acid polymerase structure has been studied by both X-ray and electron crystallography. To date, only the smaller, single subunit polymerases have been subjected to X-ray analysis, including the bacteriophage T7 RNA polymerase, which is the only RNA polymerase whose structure is known to atomic resolution. Lower resolution structures of several multisubunit polymerases have been determined by electron crystallography, including a mutant form of yeast RNA polymerase II which lacks subunits Rpb4 and Rpb7 (denoted A4/7 polymerase). All polymerase structures obtained by both X-ray and electron crystallography show a large cleft appropriate in size for binding duplex DNA, and further appear to contain a mobile arm allowing open and closed conformations of the cleft, presumably permitting entry and retention of DNA. Subunits Rpb4 and Rpb7 of RNA polymerase II form a dissociable subcomplex that has been implicated in the stress response and in the initiation of transcription. Human homologs of Rpb4 and Rpb7 have been identified.

Type
Chambers and Channels: Functional Connections in Multiprotein Complexes Studied by Single Chambers and Channels
Copyright
Copyright © Microscopy Society of America

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10. G.J J. was supported by a Medical Scientist Training Program grant (GM07365) provided by the National Institute of General Medical Sciences at the NIH. This research was funded by NIH grant AI21144 to R.D.K.Google Scholar