PMC:4502370 / 29084-29909 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4502370","sourcedb":"PMC","sourceid":"4502370","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4502370","text":"The crystal structure of yeast RNA polymerase II (Cramer et al. 2001) revealed the fold of the C-terminal segment of Rpo26 from amino acids 72 to 155, which comprises two α-helices and a β-hairpin (Figure 5). The N-terminal 71-amino-acid segment was disordered in the Pol II structure. In the recent crystal structure of yeast Pol I, the N-terminal 54-amino-acid segment of Rpo26 was disordered and the segment from amino acids 55 to 71 comprised an α-helix (Fernández-Tornero et al. 2013). A previous study had shown that deleting 42 amino acids from the N-terminus of Rpo26 did not affect the viability of yeast cells when the truncated RPO26-∆42 allele was driven by the strong GAL10 promoter in galactose-containing medium; however, deletion of 84 amino acids from the Rpo26 N-terminus was lethal (Nouraini et al. 1996a).","tracks":[{"project":"2_test","denotations":[{"id":"25911228-11313498-43354274","span":{"begin":64,"end":68},"obj":"11313498"},{"id":"25911228-24153184-43354275","span":{"begin":484,"end":488},"obj":"24153184"}],"attributes":[{"subj":"25911228-11313498-43354274","pred":"source","obj":"2_test"},{"subj":"25911228-24153184-43354275","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#eca393","default":true}]}]}}