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Repeated tertiary fold of RNA polymerase II and implications for DNA binding
1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Journal of Molecular Biology
|July 17, 1998
Summary
X-ray diffraction reveals yeast RNA polymerase II subunits Rpb1 and Rpb2 may share similar structures. DNA likely binds between these subunits, aligning with the protein's pseudo 2-fold axis.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- RNA polymerase II (Pol II) is crucial for gene transcription in eukaryotes.
- Understanding Pol II structure is key to deciphering its regulatory mechanisms.
Purpose of the Study:
- To investigate the structural relationship between the two largest subunits of yeast RNA polymerase II.
- To propose a model for DNA binding within the yeast RNA polymerase II complex.
Main Methods:
- X-ray diffraction analysis of two crystalline forms of yeast RNA polymerase II.
- Comparison of structural data with secondary structure predictions.
Main Results:
- The two largest subunits, Rpb1 and Rpb2, exhibit evidence suggesting similar protein folds.
- A potential DNA binding site located between Rpb1 and Rpb2 is identified.
- The proposed DNA binding mode involves alignment with a pseudo 2-fold axis of the enzyme.
Conclusions:
- The Rpb1 and Rpb2 subunits of yeast RNA polymerase II likely possess homologous structures.
- This structural arrangement facilitates DNA binding, a critical step in transcription initiation.
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