000046548 001__ 46548
000046548 005__ 20210121114453.0
000046548 0247_ $$2doi$$a10.1371/journal.pone.0123463
000046548 0248_ $$2sideral$$a93306
000046548 037__ $$aART-2015-93306
000046548 041__ $$aeng
000046548 100__ $$aMarcin, W.
000046548 245__ $$aThe carboxy-terminal domain of Erb1 is a seven-bladed ß-propeller that binds RNA
000046548 260__ $$c2015
000046548 5060_ $$aAccess copy available to the general public$$fUnrestricted
000046548 5203_ $$aErb1 (Eukaryotic Ribosome Biogenesis 1) protein is essential for the maturation of the ribosomal 60S subunit. Functional studies in yeast and mammalian cells showed that altogether with Nop7 and Ytm1 it forms a stable subcomplex called PeBoW that is crucial for a correct rRNA processing. The exact function of the protein within the process remains unknown. The N-terminal region of the protein includes a well conserved region shown to be involved in PeBoW complex formation whereas the carboxy-terminal half was predicted to contain seven WD40 repeats. This first structural report on Erb1 from yeast describes the architecture of a seven-bladed ß-propeller domain that revealed a characteristic extra motif formed by two a-helices and a ß-strand that insert within the second WD repeat. We performed analysis of molecular surface and crystal packing, together with multiple sequence alignment and comparison of the structure with other ß-propellers, in order to identify areas that are more likely to mediate protein-protein interactions. The abundance of many positively charged residues on the surface of the domain led us to investigate whether the propeller of Erb1 might be involved in RNA binding. Three independent assays confirmed that the protein interacted in vitro with polyuridilic acid (polyU), thus suggesting a possible role of the domain in rRNA rearrangement during ribosome biogenesis.
000046548 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/SAF2012-31405$$9info:eu-repo/grantAgreement/ES/MINECO/CTQ2013-4493$$9info:eu-repo/grantAgreement/ES/MINECO/CSD2008-00005$$9info:eu-repo/grantAgreement/EC/FP7/283570/EU/Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities/BIOSTRUCT-X
000046548 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000046548 590__ $$a3.057$$b2015
000046548 591__ $$aMULTIDISCIPLINARY SCIENCES$$b11 / 62 = 0.177$$c2015$$dQ1$$eT1
000046548 592__ $$a1.427$$b2015
000046548 593__ $$aAgricultural and Biological Sciences (miscellaneous)$$c2015$$dQ1
000046548 593__ $$aMedicine (miscellaneous)$$c2015$$dQ1
000046548 593__ $$aBiochemistry, Genetics and Molecular Biology (miscellaneous)$$c2015$$dQ1
000046548 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000046548 700__ $$aNeira, J.L.
000046548 700__ $$aBravo, J.
000046548 773__ $$g10, 4 (2015), 0123463 [22 pp]$$pPLoS One$$tPloS one$$x1932-6203
000046548 8564_ $$s2260319$$uhttps://zaguan.unizar.es/record/46548/files/texto_completo.pdf$$yVersión publicada
000046548 8564_ $$s105913$$uhttps://zaguan.unizar.es/record/46548/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000046548 909CO $$ooai:zaguan.unizar.es:46548$$particulos$$pdriver
000046548 951__ $$a2021-01-21-10:47:03
000046548 980__ $$aARTICLE