Crystal structure of RNA polymerase II from Komagataella pastoris

• DOI: 10.1016/j.bbrc.2017.04.039
• Publication Date: 2017-04-12T03:15:20Z
• Authors: Haruhiko Ehara; Takashi Umehara; Shun-ichi Sekine; Shigeyuki Yokoyama
• Keywords: Structure-Activity Relationship; 0303 health sciences; 03 medical and health sciences; Crystallography; Ascomycota; Protein Domains; Species Specificity; Protein Conformation; RNA Polymerase II

RNA polymerase II (Pol II) is a 12-subunit protein complex that conducts the transcription of mRNA and some small RNAs. In this work, the crystal structure of Pol II from the methylotropic yeast Komagataella pastoris (Pichia pastoris) was determined. While the structure is highly homologous to that of Pol II from the budding yeast Saccharomyces cerevisiae, the stalk and clamp modules of the K. pastoris Pol II displayed large inward rotations, closing the central cleft to a greater extent than in the known S. cerevisiae Pol II structures. The conformational differences reflect the inherent flexibilities of the stalk and the clamp, as additional low-resolution structures of K. pastoris Pol II in different crystal forms revealed diverse stalk and clamp orientations. Comparisons with other eukaryotic/archaeal RNA polymerase structures in the Protein Data Bank revealed the distributions of the stalk and clamp orientations. The conformational plasticity should be essential for transcriptional functions and binding various regulatory factors.