2mh2

From Proteopedia

(Difference between revisions)

Revision as of 22:39, 9 August 2018

Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of HOP2

Structural highlights

2mh2 is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Hop2, Psmc3ip, Tbpip (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HOP2_MOUSE] Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

The HOP2 protein is required for efficient double-strand break repair which ensures the proper synapsis of homologous chromosomes and normal meiotic progression. We previously showed that in vitro HOP2 shows two distinctive activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates DMC1 and RAD51 recombination activities, and the purified HOP2 alone is proficient in promoting strand invasion. The structural and biochemical basis of HOP2 action in recombination are poorly understood; therefore, they are the focus of this work. Herein, we present the solution structure of the amino-terminal portion of mouse HOP2, which contains a typical winged helix DNA-binding domain. Together with NMR spectral changes in the presence of double-stranded DNA, protein docking on DNA, and mutation analysis to identify the amino acids involved in DNA coordination, our results on the three-dimensional structure of HOP2 provide key information on the fundamental structural and biochemical requirements directing the interaction of HOP2 with DNA. These results, in combination with mutational experiments showing the role of a coiled-coil structural feature involved in HOP2 self-association, allow us to explain important aspects of the function of HOP2 in recombination.

Solution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 Protein.,Moktan H, Guiraldelli MF, Eyster CA, Zhao W, Lee CY, Mather T, Camerini-Otero RD, Sung P, Zhou DH, Pezza RJ J Biol Chem. 2014 May 23;289(21):14682-91. doi: 10.1074/jbc.M114.548180. Epub, 2014 Apr 6. PMID:24711446^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tanaka T, Nakamura T, Takagi H, Sato M. Molecular cloning and characterization of a novel TBP-1 interacting protein (TBPIP):enhancement of TBP-1 action on Tat by TBPIP. Biochem Biophys Res Commun. 1997 Oct 9;239(1):176-81. PMID:9345291 doi:http://dx.doi.org/10.1006/bbrc.1997.7447
↑ Enomoto R, Kinebuchi T, Sato M, Yagi H, Shibata T, Kurumizaka H, Yokoyama S. Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated homologous pairing. J Biol Chem. 2004 Aug 20;279(34):35263-72. Epub 2004 Jun 10. PMID:15192114 doi:http://dx.doi.org/10.1074/jbc.M402481200
↑ Pezza RJ, Petukhova GV, Ghirlando R, Camerini-Otero RD. Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the Hop2-Mnd1 complex. J Biol Chem. 2006 Jul 7;281(27):18426-34. Epub 2006 May 4. PMID:16675459 doi:http://dx.doi.org/M601073200
↑ Chi P, San Filippo J, Sehorn MG, Petukhova GV, Sung P. Bipartite stimulatory action of the Hop2-Mnd1 complex on the Rad51 recombinase. Genes Dev. 2007 Jul 15;21(14):1747-57. PMID:17639080 doi:http://dx.doi.org/21/14/1747
↑ Pezza RJ, Voloshin ON, Vanevski F, Camerini-Otero RD. Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous pairing. Genes Dev. 2007 Jul 15;21(14):1758-66. PMID:17639081 doi:http://dx.doi.org/21/14/1758
↑ Ploquin M, Petukhova GV, Morneau D, Dery U, Bransi A, Stasiak A, Camerini-Otero RD, Masson JY. Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51 recombinases. Nucleic Acids Res. 2007;35(8):2719-33. Epub 2007 Apr 10. PMID:17426123 doi:http://dx.doi.org/gkm174
↑ Moktan H, Guiraldelli MF, Eyster CA, Zhao W, Lee CY, Mather T, Camerini-Otero RD, Sung P, Zhou DH, Pezza RJ. Solution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 Protein. J Biol Chem. 2014 May 23;289(21):14682-91. doi: 10.1074/jbc.M114.548180. Epub, 2014 Apr 6. PMID:24711446 doi:http://dx.doi.org/10.1074/jbc.M114.548180

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mh2"

@@ Line 1: / Line 1: @@
 ==Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of HOP2==
 <StructureSection load='2mh2' size='340' side='right' caption='[[2mh2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2mh2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MH2 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hop2, Psmc3ip, Tbpip ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mh2 OCA], [http://pdbe.org/2mh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mh2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mh2 OCA], [http://pdbe.org/2mh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mh2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mh2 ProSAT]</span></td></tr>
 </table>
 == Function ==

2mh2

From Proteopedia

Revision as of 22:39, 9 August 2018

Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of HOP2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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