2mpu: Difference between revisions

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New page: '''Unreleased structure''' The entry 2mpu is ON HOLD Authors: Mason, K.E., Tripet, B.P., Eilers, B.J., Powell, P., Fischer, A.M., Copie, V. Description: Structural and Functional analy...
 
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'''Unreleased structure'''


The entry 2mpu is ON HOLD
==Structural and Functional analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA binding protein implicated in the regulation of barley leaf senescence and environmental adaptation==
<StructureSection load='2mpu' size='340' side='right'caption='[[2mpu]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mpu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpu OCA], [https://pdbe.org/2mpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mpu RCSB], [https://www.ebi.ac.uk/pdbsum/2mpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/J7FTI7_HORVU J7FTI7_HORVU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The timing of whole-plant senescence influences important agricultural traits such as yield and grain protein content. Post-transcriptional regulation by plant RNA-binding proteins is essential for proper control of gene expression, development, and stress responses. Here, we report the three-dimensional solution NMR structure and nucleic acid-binding properties of the barley glycine-rich RNA-binding protein HvGR-RBP1, whose transcript has been identified as being &gt;45-fold up-regulated in early-as compared to late-senescing near-isogenic barley germplasm. NMR analysis reveals that HvGR-RBP1 is a multidomain protein comprising a well-folded N-terminal RNA Recognition Motif (RRM) and a structurally disordered C-terminal glycine-rich domain. Chemical shift differences observed in 2D (1)H-(15)N correlation (HSQC) NMR spectra of full-length HvGR-RBP1 and N-HvGR-RBP1 (RRM domain only) suggest that the two domains can interact both in-trans and intramolecularly, similar to what is observed in the tobacco NtGR-RBP1 protein. Further, we show that the RRM domain of HvGR-RBP1 binds single-stranded DNA nucleotide fragments containing the consensus nucleotide sequence 5'-TTCTGX-3' with low micromolar affinity in vitro. We also demonstrate that the C-terminal glycine-rich (HvGR) domain of Hv-GR-RBP1 can interact nonspecifically with ssRNA in vitro. Structural similarities with other plant glycine-rich RNA-binding proteins suggest that HvGR-RBP1 may be multifunctional. Based on gene expression analysis following cold stress in barley and E. coli growth studies following cold shock treatment, we conclude that HvGR-RBP1 functions in a manner similar to cold-shock proteins and harbors RNA chaperone activity. HvGR-RBP1 is therefore not only involved in the regulation of barley development including senescence, but also functions in plant responses to environmental stress.


Authors: Mason, K.E., Tripet, B.P., Eilers, B.J., Powell, P., Fischer, A.M., Copie, V.
Structural and Biochemical Analysis of the Hordeum vulgare L. HvGR-RBP1 Protein, a Glycine-Rich RNA-Binding Protein Involved in the Regulation of Barley Plant Development and Stress Response.,Tripet BP, Mason KE, Eilers BJ, Burns J, Powell P, Fischer AM, Copie V Biochemistry. 2014 Dec 23;53(50):7945-60. doi: 10.1021/bi5007223. Epub 2014 Dec, 12. PMID:25495582<ref>PMID:25495582</ref>


Description: Structural and Functional analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA binding protein implicated in the regulation of barley leaf senescence and environmental adaptation recognition motif of HvRBP1 from Hordeum vulgare L. (barley)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mpu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hordeum vulgare]]
[[Category: Large Structures]]
[[Category: Copie V]]
[[Category: Eilers BJ]]
[[Category: Fischer AM]]
[[Category: Mason KE]]
[[Category: Powell P]]
[[Category: Tripet BP]]