Cargando…

Mechanism of Ribonuclease III Catalytic Regulation by Serine Phosphorylation

Ribonuclease III (RNase III) is a conserved, gene-regulatory bacterial endonuclease that cleaves double-helical structures in diverse coding and noncoding RNAs. RNase III is subject to multiple levels of control, reflective of its global regulatory functions. Escherichia coli (Ec) RNase III catalyti...

Descripción completa

Detalles Bibliográficos
Autores principales:	Gone, Swapna, Alfonso-Prieto, Mercedes, Paudyal, Samridhdi, Nicholson, Allen W.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group 2016
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858673/ https://www.ncbi.nlm.nih.gov/pubmed/27150669 http://dx.doi.org/10.1038/srep25448

Ejemplares similares

Combined computational and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB
por: Paudyal, Samridhdi, et al.
Publicado: (2015)

Ribonuclease III mechanisms of double-stranded RNA cleavage
por: Nicholson, Allen W
Publicado: (2014)

Catalytic mechanism of Escherichia coli ribonuclease III: kinetic and inhibitor evidence for the involvement of two magnesium ions in RNA phosphodiester hydrolysis
por: Sun, Weimei, et al.
Publicado: (2005)

Mouse ribonuclease III. cDNA structure, expression analysis, and chromosomal location
por: Fortin, Kristine R, et al.
Publicado: (2002)

Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates
por: Shi, Zhongjie, et al.
Publicado: (2011)

HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors
por: Beilhartz, Greg L., et al.
Publicado: (2010)

Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III
por: Pertzev, Alexandre V., et al.
Publicado: (2006)

The catalytic efficiency of yeast ribonuclease III depends on substrate specific product release rate
por: Comeau, Marc-Andre, et al.
Publicado: (2016)

The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H
por: Pang, Jing, et al.
Publicado: (2022)

Data on the phosphorylation state of the catalytic serine of enzymes in the α-D-phosphohexomutase superfamily
por: Lee, Yingying, et al.
Publicado: (2016)

Phosphorylation of the RNase III enzyme Drosha at Serine300 or Serine302 is required for its nuclear localization
por: Tang, Xiaoli, et al.
Publicado: (2010)

STUDIES ON THE FUNCTION OF INTRACELLULAR RIBONUCLEASES : III. The Relationship of the Ribonuclease Activity of Rat Liver Microsomes to their Biological Activity
por: Roth, Jay S.
Publicado: (1960)

Regulation of divalent metal transporter-1 by serine phosphorylation
por: Seo, Young Ah, et al.
Publicado: (2016)

An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract
por: Spencer, John David, et al.
Publicado: (2013)

Evolutionary patterns of phosphorylated serines
por: Kurmangaliyev, Yerbol Z, et al.
Publicado: (2011)

The Production of Extracellular Proteins Is Regulated by Ribonuclease III via Two Different Pathways in Staphylococcus aureus
por: Liu, Yu, et al.
Publicado: (2011)

Regulation of the small regulatory RNA MicA by ribonuclease III: a target-dependent pathway
por: Viegas, Sandra C., et al.
Publicado: (2011)

Catalytic Knockdown of miR-21 by Artificial Ribonuclease: Biological Performance in Tumor Model
por: Patutina, Olga A., et al.
Publicado: (2019)

Serine phosphorylation regulates paxillin turnover during cell migration
por: Abou Zeid, Nancy, et al.
Publicado: (2006)

An allosteric regulation mechanism of Arabidopsis Serine/Threonine kinase 1 (SIK1) through phosphorylation
por: Mu, Junxi, et al.
Publicado: (2021)

Phosphorylation of histone H3 serine 28 modulates RNA polymerase III-dependent transcription
por: Zhang, Qingsong, et al.
Publicado: (2011)

CRYSTALLINE RIBONUCLEASE
por: Kunitz, M.
Publicado: (1940)

A Practical Preparation of Ribonuclease-S and the Action of Subtilisin on Ribonuclease-B
por: Gordillo, Guido, et al.
Publicado: (1962)

Site-Selective Artificial Ribonucleases: Oligonucleotide Conjugates Containing Multiple Imidazole Residues in the Catalytic Domain
por: Beloglazova, Natalia G., et al.
Publicado: (2011)

Ring nucleases deactivate Type III CRISPR ribonucleases by degrading cyclic oligoadenylate
por: Athukoralage, Januka S, et al.
Publicado: (2018)

Phosphorylation on TRPV4 Serine 824 Regulates Interaction with STIM1
por: Shin, Sung H, et al.
Publicado: (2015)

Serine phosphorylation regulates the P-type potassium pump KdpFABC
por: Sweet, Marie E, et al.
Publicado: (2020)

Serine 165 phosphorylation of SHARPIN regulates the activation of NF-κB
por: Thys, An, et al.
Publicado: (2020)

Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T(1) to carboxyl peptidases
por: TAKAHASHI, Kenji
Publicado: (2013)

Information available at cut rates: structure and mechanism of ribonucleases
por: Worrall, Jonathan AR, et al.
Publicado: (2007)

Ribonucleases and bacterial virulence
por: Lawal, Abidat, et al.
Publicado: (2011)

Ribonucleases as antiviral agents
por: Ilinskaya, O. N., et al.
Publicado: (2014)

The Nϵ‐Rule for Serine, but Not Cysteine Catalytic Triads
por: Czapinska, Honorata, et al.
Publicado: (2022)

Hunting for Serine 276-Phosphorylated p65
por: Spooren, Anneleen, et al.
Publicado: (2010)

A Type III CRISPR Ancillary Ribonuclease Degrades Its Cyclic Oligoadenylate Activator
por: Athukoralage, Januka S., et al.
Publicado: (2019)

The ribonuclease Dis3 is an essential regulator of the developmental transcriptome
por: Hou, Dezhi, et al.
Publicado: (2012)

ERK2 phosphorylation of serine 77 regulates Bmf pro-apoptotic activity
por: Shao, Y, et al.
Publicado: (2012)

Phosphorylation of Serine 106 in Asef2 Regulates Cell Migration and Adhesion Turnover
por: Evans, J. Corey, et al.
Publicado: (2014)

The phosphorylation of sorting nexin 5 at serine 226 regulates retrograde transport and macropinocytosis
por: Itai, Nao, et al.
Publicado: (2018)

SAT-139 STAT5A Regulation by Serine Phosphorylation in Breast Cancer
por: Woock, Alicia E, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_c8t7o72hub6c34qn65de7rqhpt