In higher eukaryotes, the dsRNA binding proteins (dsRBPs) assist the corresponding Dicer in the cleavage of dsRNA precursors to effect post-transcriptional gene regulation through RNA interference. In contrast, the DRB7.2:DRB4 complex in Arabidopsis thaliana acts as a potent inhibitor of Dicer-like 3 (DCL3) processing by sequestering endogenous inverted-repeat dsRNA precursors. DRB7.2 possesses a single dsRNA Binding Domain (dsRBD) flanked by unstructured N- and C-terminal regions. Whereas, DRB4...
[NMR paper] NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex gamma subunit
NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex gamma subunit
The E. coli ? clamp loader is a pentameric complex of ?, ?' and three ? subunits that opens and loads ?-clamp proteins onto DNA in an ATP-dependent process essential for efficient DNA replication. ATP binding to the ? subunits promotes conformational changes that enable the clamp loader to bind and open the ring-shaped ?-clamp homodimer. Here we report the nearly complete backbone and side-chain ąH, ^(13)C and ^(15)N NMR resonance assignments of the 242-residue truncated ? subunit...
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03-24-2021 11:20 PM
Solution NMR Structure and Backbone Dynamics of PartiallyDisordered Arabidopsis thaliana Phloem Protein 16-1,a Putative mRNA Transporter
Solution NMR Structure and Backbone Dynamics of PartiallyDisordered Arabidopsis thaliana Phloem Protein 16-1,a Putative mRNA Transporter
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01071/20180125/images/medium/bi-2017-01071p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01071
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01-27-2018 12:19 AM
Iron Binding Properties of Recombinant Class A ProteinDisulfide Isomerase from Arabidopsis thaliana
Iron Binding Properties of Recombinant Class A ProteinDisulfide Isomerase from Arabidopsis thaliana
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01257/20170407/images/medium/bi-2016-012576_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01257
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04-08-2017 10:57 AM
Water–Polysaccharide Interactions in the Primary Cell Wall of Arabidopsis thaliana from Polarization Transfer Solid-State NMR
Water–Polysaccharide Interactions in the Primary Cell Wall of Arabidopsis thaliana from Polarization Transfer Solid-State NMR
Paul B. White, Tuo Wang, Yong Bum Park, Daniel J. Cosgrove and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504108h/aop/images/medium/ja-2014-04108h_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504108h
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http://feeds.feedburner.com/~r/acs/jacsat/~4/7abtnNxi-xg
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07-15-2014 09:25 AM
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
Biomol NMR Assign. 2011 May 8;
Authors: Mylne JS, Mas C, Hill JM
VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39*kDa protein...
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05-10-2011 05:11 PM
[NMR paper] NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana S
NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Related Articles NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Chembiochem. 2003 Mar 3;4(2-3):171-80
Authors: Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
Zinc finger domains of the classical type represent the most abundant DNA binding domains in eukaryotic transcription factors. Plant proteins...
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11-24-2010 09:01 PM
[NMR paper] NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Related Articles NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Biochemistry. 2002 Oct 15;41(41):12284-96
Authors: Zhao Q, Chae YK, Markley JL
The three-dimensional structure of the precursor form of the Arabidopsis thaliana trypsin inhibitor (ATT(p), GenBank entry Z46816), a 68-residue (approximately 7.5 kDa) rapeseed class proteinase inhibitor, has been determined in solution at pH 5.0 and 25 degrees C by multinuclear magnetic resonance...