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9UKS

CryoEM structure of the T.thermophilus transcription initiation complex in the presence of Gp4A, -1 dA in the template DNA strand

Summary for 9UKS
Entry DOI10.2210/pdb9uks/pdb
EMDB information64253
DescriptorDNA-directed RNA polymerase subunit alpha, ZINC ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total)
Functional Keywordscomplex, transcription
Biological sourceThermus thermophilus HB8
More
Total number of polymer chains8
Total formula weight457232.34
Authors
Duan, W.,Kaushik, A.,Serganov, A. (deposition date: 2025-04-18, release date: 2025-10-22, Last modification date: 2025-10-29)
Primary citationDuan, W.,Kaushik, A.,Unarta, I.C.,Wu, Y.,Liu, M.M.J.,Weaver, J.W.,Wang, B.,Rice, W.J.,Luciano, D.J.,Belasco, J.G.,Huang, X.,Nudler, E.,Serganov, A.
Molecular basis for noncanonical transcription initiation from Np 4 A alarmones.
Nat.Chem.Biol., 2025
Cited by
PubMed Abstract: Stress-induced dinucleoside tetraphosphates (NpNs, where N is adenosine, guanosine, cytosine or uridine) are ubiquitous in living organisms, yet their function has been largely elusive for over 50 years. Recent studies have revealed that RNA polymerase can influence the cellular lifetime of transcripts by incorporating these alarmones into RNA as 5'-terminal caps. Here we present structural and biochemical data that reveal the molecular basis of noncanonical transcription initiation from NpAs by Escherichia coli and Thermus thermophilus RNA polymerases. Our results show the influence of the first two nucleotide incorporation steps on capping efficiency and the different interactions of NpAs with transcription initiation complexes. These data provide critical insights into the substrate selectivity that dictates levels of Np capping in bacterial cells.
PubMed: 41094128
DOI: 10.1038/s41589-025-02044-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.33 Å)
Structure validation

243911

數據於2025-10-29公開中

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