000170068 001__ 170068
000170068 005__ 20260316092630.0
000170068 0247_ $$2doi$$a10.1002/pro.70517
000170068 0248_ $$2sideral$$a148597
000170068 037__ $$aART-2026-148597
000170068 041__ $$aeng
000170068 100__ $$aNeira, José L.
000170068 245__ $$aUnveiling nuclear localization signals in human arginine deiminase proteins
000170068 260__ $$c2026
000170068 5060_ $$aAccess copy available to the general public$$fUnrestricted
000170068 5203_ $$aArginine iminohydrolases are a family of enzymes involved in the conversion of arginine to citrulline. There are five isoforms in humans (PADI1, 2, 3, 4, and 6). Some of them are observed experimentally in the cytoplasm and in the nucleus of the cell; for moving to the latter location, they must pass through the cell nuclear membrane by using the translocation machinery, mainly formed by the proteins named importins. We have previously described and characterized the isolated PADI4 nuclear localization sequences (NLSs) and their binding to importin α3 (Impα3). By using theoretical predictors, here we foretold the existence of several NLSs in isoforms PADI1, PADI2, and PADI3. These predicted polypeptide regions were chemically synthesized, and the soluble ones were conformationally characterized in isolation. We studied their ability to bind Impα3 and its truncated species (ΔImpα3) without the importin binding domain, by using several biophysical techniques and molecular simulations. The isolated peptides were disordered and monomeric in solution. Moreover, all of them were capable of binding to both importin species with affinities in the low micromolar range, and targeting the canonical NLS binding site for cargo proteins. These findings suggest that the predicted NLS regions could be the sites for the binding of the corresponding intact PADI protein to importin, and therefore, any of the PADI enzymes could be translocated into the nucleus.
000170068 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B25-20R$$9info:eu-repo/grantAgreement/ES/DGA/E45-20R$$9info:eu-repo/grantAgreement/ES/MICINN/AEI/PID2021-127296OB-I00
000170068 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttps://creativecommons.org/licenses/by/4.0/deed.es
000170068 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000170068 700__ $$0(orcid)0000-0001-5664-1729$$aAbian, Olga$$uUniversidad de Zaragoza
000170068 700__ $$0(orcid)0000-0001-5702-4538$$aVelazquez-Campoy, Adrián$$uUniversidad de Zaragoza
000170068 700__ $$aRizzuti, Bruno
000170068 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000170068 773__ $$g35, 4 (2026), [20 pp.]$$pProtein sci.$$tProtein science$$x0961-8368
000170068 8564_ $$s3699649$$uhttps://zaguan.unizar.es/record/170068/files/texto_completo.pdf$$yVersión publicada
000170068 8564_ $$s2420693$$uhttps://zaguan.unizar.es/record/170068/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000170068 909CO $$ooai:zaguan.unizar.es:170068$$particulos$$pdriver
000170068 951__ $$a2026-03-16-08:18:01
000170068 980__ $$aARTICLE