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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F12%3A00380982%21RIV13-GA0-61388971
rdf:type
skos:Concept n14:Vysledek
dcterms:description
Based on sequence similarity, we identified a homologue of the human RanBPM in Arabidopsis thaliana. AtRanBPM protein has highly conserved SPRY, LisH, CTLH and CRA domains. Cell fractionation showed that endogenous AtRanBPM or expressed GFP-AtRanBPM are mainly cytoplasmic proteins with only a minor portion detectable in microsomal fractions. AtRanBPM was identified predominantly in the form of soluble cytoplasmic complexes similar to 230 - 500 kDa in size. Immunopurification of AtRanBPM followed by mass spectrometric analysis identified proteins containing LisH and CRA domains; LisH, CRA, RING-U-box domains and a transducin/WD40 repeats in a complex with AtRanBPM. Homologues of identified proteins are known to be components of the C-terminal to the LisH motif (CTLH) complexes in humans and budding yeast. Microscopic analysis of GFP-AtRanBPM in vivo and immunofluorescence localization of endogenous AtRanBPM protein in cultured cells and seedlings of Arabidopsis showed mainly cytoplasmic and nuclear localization. Absence of colocalization with.-tubulin was consistent with the biochemical data and suggests another than a centrosomal role of the AtRanBPM protein. Conclusion: We showed that as yet uncharacterized Arabidopsis RanBPM protein physically interacts with LisH-CTLH domain-containing proteins. The newly identified high molecular weight cytoplasmic protein complexes of AtRanBPM showed homology with CTLH types of complexes described in mammals and budding yeast. Although the exact functions of the CTLH complexes in scaffolding of protein degradation, in protein interactions and in signalling from the periphery to the cell centre are not yet fully understood, structural conservation of the complexes across eukaryotes suggests their important biological role. Based on sequence similarity, we identified a homologue of the human RanBPM in Arabidopsis thaliana. AtRanBPM protein has highly conserved SPRY, LisH, CTLH and CRA domains. Cell fractionation showed that endogenous AtRanBPM or expressed GFP-AtRanBPM are mainly cytoplasmic proteins with only a minor portion detectable in microsomal fractions. AtRanBPM was identified predominantly in the form of soluble cytoplasmic complexes similar to 230 - 500 kDa in size. Immunopurification of AtRanBPM followed by mass spectrometric analysis identified proteins containing LisH and CRA domains; LisH, CRA, RING-U-box domains and a transducin/WD40 repeats in a complex with AtRanBPM. Homologues of identified proteins are known to be components of the C-terminal to the LisH motif (CTLH) complexes in humans and budding yeast. Microscopic analysis of GFP-AtRanBPM in vivo and immunofluorescence localization of endogenous AtRanBPM protein in cultured cells and seedlings of Arabidopsis showed mainly cytoplasmic and nuclear localization. Absence of colocalization with.-tubulin was consistent with the biochemical data and suggests another than a centrosomal role of the AtRanBPM protein. Conclusion: We showed that as yet uncharacterized Arabidopsis RanBPM protein physically interacts with LisH-CTLH domain-containing proteins. The newly identified high molecular weight cytoplasmic protein complexes of AtRanBPM showed homology with CTLH types of complexes described in mammals and budding yeast. Although the exact functions of the CTLH complexes in scaffolding of protein degradation, in protein interactions and in signalling from the periphery to the cell centre are not yet fully understood, structural conservation of the complexes across eukaryotes suggests their important biological role.
dcterms:title
Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes
skos:prefLabel
Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes
skos:notation
RIV/61388971:_____/12:00380982!RIV13-GA0-61388971
n14:predkladatel
n15:ico%3A61388971
n3:aktivita
n18:P n18:Z
n3:aktivity
P(GA204/07/1169), P(GAP501/12/2333), P(GP204/09/P155), P(IAA500200719), P(LC06034), P(LC545), Z(AV0Z50200510), Z(AV0Z50380511)
n3:cisloPeriodika
83
n3:dodaniDat
n19:2013
n3:domaciTvurceVysledku
n7:2185148 n7:8652287 n7:9066586 n7:6282520
n3:druhVysledku
n16:J
n3:duvernostUdaju
n5:S
n3:entitaPredkladatele
n17:predkladatel
n3:idSjednocenehoVysledku
142288
n3:idVysledku
RIV/61388971:_____/12:00380982
n3:jazykVysledku
n13:eng
n3:klicovaSlova
Arabidopsis homologue of RanBPM; CTLH-complex; LisH-CTLH domain proteins
n3:klicoveSlovo
n12:Arabidopsis%20homologue%20of%20RanBPM n12:LisH-CTLH%20domain%20proteins n12:CTLH-complex
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[CA81E8498218]
n3:nazevZdroje
BMC Plant Biology
n3:obor
n11:EB
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
8
n3:projekt
n9:LC06034 n9:LC545 n9:GAP501%2F12%2F2333 n9:GP204%2F09%2FP155 n9:IAA500200719 n9:GA204%2F07%2F1169
n3:rokUplatneniVysledku
n19:2012
n3:svazekPeriodika
12
n3:tvurceVysledku
Petrovská, Beáta Váchová, Lenka Kočárová, Gabriela Halada, Petr Binarová, Pavla Tomaštíková, Eva Cenklová, Věra Kohoutová, Lucie
n3:wos
000307098700001
n3:zamer
n4:AV0Z50200510 n4:AV0Z50380511
s:issn
1471-2229
s:numberOfPages
14
n20:doi
10.1186/1471-2229-12-83