Low resolution structure of the human alpha 4 protein (IgBP1) and studies on the stability of alpha 4 and of its yeast ortholog Tap42

dc.creatorSmetana, JHC
dc.creatorOliveira, CLP
dc.creatorJablonka, W
dc.creatorPertinhez, TA
dc.creatorCarneiro, FRG
dc.creatorMontero-Lomeli, M
dc.creatorTorriani, I
dc.creatorZanchin, NIT
dc.date2006
dc.dateAPR
dc.date2014-11-16T14:01:21Z
dc.date2015-11-26T17:25:18Z
dc.date2014-11-16T14:01:21Z
dc.date2015-11-26T17:25:18Z
dc.date.accessioned2018-03-29T00:12:34Z
dc.date.available2018-03-29T00:12:34Z
dc.identifierBiochimica Et Biophysica Acta-proteins And Proteomics. Elsevier Science Bv, v. 1764, n. 4, n. 724, n. 734, 2006.
dc.identifier1570-9639
dc.identifierWOS:000237878200009
dc.identifier10.1016/j.bbapap.2006.01.018
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/52746
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/52746
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/52746
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1284290
dc.descriptionThe yeast Tap42 and mammalian alpha 4 proteins belong to a highly conserved family of regulators of the type 2A phosphatases, which participate in the rapamycin-sensitive signaling pathway, connecting nutrient availability to cell growth. The mechanism of regulation involves binding of Tap42 to Sit4 and PPH21/22 in yeast and binding of a4 to the catalytic subunits of type 2A-related phosphatases PP2A, PP4 and PP6 in mammals. Both recombinant proteins undergo partial proteolysis, generating stable N-terminal fragments. The full-length proteins and a4 C-terminal deletion mutants at amino acids 222 (alpha 4 Delta 222), 236 (alpha 4 Delta 236) and 254 (alpha 4 Delta 254) were expressed in E. coli. alpha 4 Delta 254 undergoes proteolysis, producing a fragment similar to the one generated by full-length a4, whereas alpha 4 Delta 222 and alpha 4 Delta 236 are highly stable proteins. alpha 4 and Tap42 show alpha-helical circular dichroism spectra, as do their respective N-terminal proteolysis resistant products. The cloned truncated proteins alpha 4 Delta 222 and alpha 4 Delta 236, however, possess a higher content of a-helix, indicating that the C-terminal region is less structured, which is consistent with its higher sensitivity to proteolysis. In spite of their higher secondary structure content, alpha 4 Delta 222 and alpha 4 Delta 236 showed thermal unfolding kinetics similar to the full-length alpha 4. Based on small angle X-ray scattering (SAXS), the calculated radius of gyration for alpha 4 and Tap42 were 41.2 +/- 0.8 angstrom and 42.8 +/- 0.7 angstrom and their maximum dimension similar to 142 angstrom and similar to 147 angstrom, respectively. The radii of gyration for alpha 4 Delta 222 and alpha 4 Delta 236 were 21.6 +/- 0.3 angstrom and 25.7 +/- 0.2 angstrom, respectively. Kratky plots show that all studied proteins show variable degree of compactness. Calculation of model structures based on SAXS data showed that alpha 4 Delta 222 and alpha 4 Delta 236 proteins have globular conformation, whereas alpha 4 and Tap42 exhibit elongated shapes. (c) 2006 Elsevier B.V. All rights reserved.
dc.description1764
dc.description4
dc.description724
dc.description734
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationBiochimica Et Biophysica Acta-proteins And Proteomics
dc.relationBBA-Proteins Proteomics
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectTap42 protein family
dc.subjectrapamycin signaling pathway
dc.subjectsmall angle X-ray scattering
dc.subjectSmall-angle Scattering
dc.subjectNatively Unfolded Proteins
dc.subjectPhosphatase 2a
dc.subjectCatalytic Subunit
dc.subjectBiological Macromolecules
dc.subjectSignal-transduction
dc.subjectIntrinsic Disorder
dc.subjectRegulatory Subunit
dc.subjectMolecular-cloning
dc.subjectAssociation
dc.titleLow resolution structure of the human alpha 4 protein (IgBP1) and studies on the stability of alpha 4 and of its yeast ortholog Tap42
dc.typeArtículos de revistas


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