Related ArticlesNMR resonance assignments of the FinO-domain of the RNA chaperone RocC.
Biomol NMR Assign. 2020 Nov 11;:
Authors: Eidelpes R, Kim HJ, Glover JNM, Tollinger M
Abstract
In prokaryotic species, gene expression is commonly regulated by small, non-coding RNAs (sRNAs). In the gram-negative bacterium Legionella pneumophila, the regulatory, trans-acting sRNA molecule RocR base pairs with a complementary sequence in the 5'-untranslated region of mRNAs encoding for proteins in the bacterial DNA uptake system, thereby controlling natural competence. Sense-antisense duplexing of RocR with targeted mRNAs is mediated by the recently described RNA chaperone RocC. RocC contains a 12*kDa FinO-domain, which acts as sRNA binding platform, along with an extended C-terminal segment that is predicted to be mostly disordered but appears to be required for repression of bacterial competence. In this work we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of RocC's FinO-domain by solution NMR spectroscopy. The chemical shift data for this protein indicate a mixed ?/? fold that is reminiscent of FinO from Escherichia coli. Our NMR resonance assignments provide the basis for a comprehensive analysis of RocC's chaperoning mechanism on a structural level.
PMID: 33179208 [PubMed - as supplied by publisher]
[NMR paper] NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1.
NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1.
Related Articles NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1.
Biomol NMR Assign. 2017 Aug 22;:
Authors: Führer S, Ahammer L, Ausserbichler A, Scheffzek K, Dunzendorfer-Matt T, Tollinger M
Abstract
Neurofibromin and Sprouty-related EVH1 domain-containing protein 1 (Spred1) both act as negative regulators of the mitogen-activated protein kinase pathway and are associated with the rare...
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[NMR paper] NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
Biomol NMR Assign. 2017 Mar 06;:
Authors: Alyami EM, Rizzo AA, Beuning PJ, Korzhnev DM
Abstract
The ?-clamp protein and the ? clamp loader complex are essential...
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[NMR paper] Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Related Articles Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
Biomol NMR Assign. 2017 Feb 28;:
Authors: Conroy BS, Weiss ER, Smith SP, Langelaan DN
Abstract
Krüppel-like factor 4 (KLF4) is a transcription factor involved in diverse biological processes, including development, cellular differentiation and proliferation, and maintenance of tissue homeostasis. KLF4 has...
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[NMR paper] NMR resonance assignments of caspase recruitment domain of RIP2 kinase.
NMR resonance assignments of caspase recruitment domain of RIP2 kinase.
NMR resonance assignments of caspase recruitment domain of RIP2 kinase.
Biomol NMR Assign. 2016 Mar 16;
Authors: Lin Z
Abstract
Receptor interacting protein-2, RIP2, is a serine/threonine kinase and has sequence homology to RIP. It functions as an adaptor molecule for some members from the tumor necrosis factor receptor family and mediates divergent signaling pathways including NF-?B activation and cell death. RIP2 contains an N-terminal kinases domain and a...
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03-18-2016 05:23 PM
[NMR paper] NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK.
NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK.
Related Articles NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK.
J Biomol NMR. 2005 Jan;31(1):65
Authors: Devany M, Matsuo H
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[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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[NMR paper] 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2
1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
Related Articles 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
J Biomol NMR. 1998 May;11(4):457-8
Authors: Veeraraghavan S, Mello CC, Lee KM, Androphy EJ, Baleja JD
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[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
J Biomol NMR. 1994 Nov;4(6):845-58
Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD
The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...