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Titolo:
Human ribosomal protein L5 contains defined nuclear localization and export signals
Autore:
Rosorius, O; Fries, B; Stauber, RH; Hirschmann, N; Bevec, D; Hauber, J;
Indirizzi:
Univ Erlangen Nurnberg, Inst Clin & Mol Virol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany Novartis Res Inst, Dept Immunol, A-1235 Vienna, Austria Novartis Res InstVienna Austria A-1235 Immunol, A-1235 Vienna, Austria
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 16, volume: 275, anno: 2000,
pagine: 12061 - 12068
SICI:
0021-9258(20000421)275:16<12061:HRPLCD>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS REV; HIV-1 REV; XENOPUS OOCYTES; LIVING CELLS; NUCLEOCYTOPLASMIC TRANSPORT; NUCLEOLAR LOCALIZATION; ACTIVATION DOMAIN; GENE-EXPRESSION; RNA; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Hauber, J Univ Erlangen Nurnberg, Inst Clin & Mol Virol, Schlossgarten 4, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Schlossgarten 4 Erlangen Germany D-91054
Citazione:
O. Rosorius et al., "Human ribosomal protein L5 contains defined nuclear localization and export signals", J BIOL CHEM, 275(16), 2000, pp. 12061-12068

Abstract

Ribosomal protein L5 is part of the 60 S ribosomal subunit and localizes in both the cytoplasm and the nucleus of eukaryotic cells, accumulating particularly in the nucleoli. L5 is known to bind specifically to 5 S rRNA and is involved in nucleocytoplasmic transport of this rRNA, Here, we report a detailed analysis of the domain organization of the human ribosomal proteinL5. We show that a signal that mediates nuclear import and nucleolar localization maps to amino acids 21-37 within the 297-amino acid L5 protein. Furthermore, carboxyl-terminal residues at positions 255-297 serve as an additional nuclear/nucleolar targeting signal. Domains involved in 5 S rRNA binding are located at both the amino terminus and the carboxyl terminus of L5,Microinjection studies in somatic cells demonstrate that a nuclear export signal (NES) that maps to amino acids 101-111 resides in the central regionof L5. This NES is characterized by a pronounced clustering of critical leucine residues, which creates a peptide motif not previously observed in other leucine-rich NESs. Finally, we present a refined model of the multidomain structure of human ribosomal protein L5.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 05:28:45