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Nucleic Acids Research
Nucleic Acids Research, In press, ⟨10.1093/nar/gkac346⟩
Nucleic Acids Research, In press, ⟨10.1093/nar/gkac346⟩
Promoters and enhancers are sites of transcription initiation (TSSs) and carry active histone modifications, including H3K4me1, H3K4me3, and H3K27ac. Yet, the principles governing the boundaries of such regulatory elements are still poorly characteri
Published in:
Nucleic Acids Research. 50:5029-5046
Bacterial mRNAs have short life cycles, in which transcription is rapidly followed by translation and degradation within seconds to minutes. The resulting diversity of mRNA molecules across different life-cycle stages impacts their functionality but
Published in:
Nucleic Acids Research. 50:4042-4053
Mtr4 is a eukaryotic RNA helicase required for RNA decay by the nuclear exosome. Previous studies have shown how RNA enroute to the exosome threads through the highly conserved helicase core of Mtr4. Mtr4 also contains an arch domain, although detail
Published in:
Nucleic Acids Research. 50:2973-2985
Serine integrases are emerging as one of the most powerful biological tools for synthetic biology. They have been widely used across genome engineering and genetic circuit design. However, developing serine integrase-based tools for directly/precisel
Published in:
Nucleic Acids Research
Many bacteria use cyclic dimeric guanosine monophosphate (c-di-GMP) to control changes in lifestyle. The molecule, synthesised by proteins having diguanylate cyclase activity, is often a signal to transition from motile to sedentary behaviour. In Vib
Author/Creator:
Julian A. Zagalak, Mahmoud-Reza Rafiee, Karen Davey, Sviatoslav Sidorov, Sebastian Steinhauser, Nicholas M. Luscombe, Jernej Ule
Published in:
Nucleic Acids Research
bioRxiv
bioRxiv
RNA-binding proteins (RBPs) play diverse roles in regulating co-transcriptional RNA-processing and chromatin functions, but our knowledge of the repertoire of chromatin-associated RBPs (caRBPs) and their interactions with chromatin remains limited. H
Author/Creator:
Yaoyong Li, Samantha Carrera, Andrew D. Sharrocks, Karol Nowicki-Osuch, Shen Hsi Yang, Syed Murtuza Baker, David G. Spiller, Amanda O'Donnell
Published in:
Nucleic Acids Research
Carrera, S, O'Donnell, A, Li, Y, Nowicki-Osuch, K, Yang, S-H, Baker, S M, Spiller, D & Sharrocks, A 2021, ' Complexities in the role of acetylation dynamics in modifying inducible gene activation parameters. ', Nucleic Acids Res, vol. 49, no. 22, pp. 12744–12756 . https://doi.org/10.1093/nar/gkab1176
Carrera, S, O'Donnell, A, Li, Y, Nowicki-Osuch, K, Yang, S-H, Baker, S M, Spiller, D & Sharrocks, A 2021, ' Complexities in the role of acetylation dynamics in modifying inducible gene activation parameters. ', Nucleic Acids Res, vol. 49, no. 22, pp. 12744–12756 . https://doi.org/10.1093/nar/gkab1176
High levels of histone acetylation are associated with the regulatory elements of active genes, suggesting a link between acetylation and gene activation. We revisited this model, in the context of EGF-inducible gene expression and found that rather
Published in:
Nucleic Acids Research
When vertebrate replisomes from neighboring origins converge, the Mcm7 subunit of the replicative helicase, CMG, is ubiquitylated by the E3 ubiquitin ligase, CRL2Lrr1. Polyubiquitylated CMG is then disassembled by the p97 ATPase, leading to replicati
Author/Creator:
Richard J. Maraia, Alan C. Kessler
Published in:
Nucleic Acids Res
A 1969 report that described biochemical and activity properties of the three eukaryotic RNA polymerases revealed Pol III as highly distinguishable, even before its transcripts were identified. Now known to be the most complex, Pol III contains sever
Author/Creator:
Rafael Molina, Anne Louise Grøn Jensen, Stefano Stella, Guillermo Montoya, Blanca López-Méndez, Javier Marchena-Hurtado
Published in:
Nucleic Acids Research
Molina Monterrubio, R A, Jensen, A L G, Marchena-Hurtado, J, López-Méndez, B, Stella, S & Montoya, G 2021, ' Structural basis of cyclic oligoadenylate degradation by ancillary Type III CRISPR-Cas ring nucleases ', Nucleic Acids Research, vol. 49, no. 21, pp. 12577-12590 . https://doi.org/10.1093/nar/gkab1130
Molina Monterrubio, R A, Jensen, A L G, Marchena-Hurtado, J, López-Méndez, B, Stella, S & Montoya, G 2021, ' Structural basis of cyclic oligoadenylate degradation by ancillary Type III CRISPR-Cas ring nucleases ', Nucleic Acids Research, vol. 49, no. 21, pp. 12577-12590 . https://doi.org/10.1093/nar/gkab1130
Type III CRISPR-Cas effector systems detect foreign RNA triggering DNA and RNA cleavage and synthesizing cyclic oligoadenylate molecules (cA) in their Cas10 subunit. cAs act as a second messenger activating auxiliary nucleases, leading to an indiscri