The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs.

Lee, Wen-Ching; Xue, Zhixiong; Melese, Teri

doi:10.1083/jcb.113.1.1

Cited by 171 publications

(112 citation statements)

References 61 publications

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“…The polypeptide, termed Nopp52, exhibits a highly modular domain structure with alternating acidic/basic repeats distinguishing its amino-terminal half. A similar organization of alternating acidic/basic stretches has also been described in many nucleolar proteins including nucleolin, NSR1, NpI46, Noppl40, and B23/No38 (Dingwall et al, 1987;Lapeyre et al, 1987;Lee et al, 1991;Meier and Blobel, 1992;Shan et al, 1994). Many of this class of polypeptides, including Nopp52, have aberrantly slow mobility in SDS gels and are phosphorylated by CKII.…”

Section: Discussionmentioning

confidence: 95%

“…Interestingly the two, vertebrate nucleolin and yeast NSR1, are localized to nucleoli (Lapeyre et al, 1987;Lee et al, 1991) as is Nopp52 (see below). However, there exist several clear differences between them.…”

Section: Nopp-52 An Abundant Macronuclearmentioning

confidence: 99%

“…In this study, we report the identification and characterization of a prominent macronuclearspecific phosphoprotein enriched in Tetrahymena nucleoli. The cDNA sequence encoding this 52-kDa polypeptide (termed Nopp52) predicts a domain structure similar to other nucleolar proteins, especially vertebrate nucleolin and yeast NSR1 (Lapeyre et al, 1987;Lee et al, 1991). In situ hybridization to rDNA and immunocytochemical localization of Nopp52 indicates these components are colocalized in nucleoli.…”

Section: Introductionmentioning

confidence: 99%

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An abundant nucleolar phosphoprotein is associated with ribosomal DNA in Tetrahymena macronuclei.

McGrath

Smothers

Dadd

et al. 1997

MBoC

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Section: Discussionmentioning

confidence: 95%

Section: Nopp-52 An Abundant Macronuclearmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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An abundant nucleolar phosphoprotein is associated with ribosomal DNA in Tetrahymena macronuclei.

McGrath

Smothers

Dadd

et al. 1997

MBoC

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“…Preliminary studies by Finlay and Forbes [19901 suggest the presence of 8-10 different possible NLSreceptor molecules associated with the nuclear pore. NLS-binding polypeptides, shuttling between the cytoplasm and the nucleoplasm or the nucleolus, may be present in addition to those associated with the pore [Borer et al, 1989;Yamasaki et al, 1989;Adam et al, 1989;Blobel, 1990, 1992;Lee et al, 1991;Li et al, 19921.…”

Section: Nls-binding Proteinsmentioning

confidence: 99%

Putative nuclear localization signals (NLS) in protein transcription factors

Boulikas

1994

J of Cellular Biochemistry

188

121

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We have recognized about ten distinct forms of strongly basic hexapeptides, containing at least four arginines and lysines, characteristic of nuclear proteins among all eukaryotic species, including yeast, plants, flies and mammals. These basic hexapeptides are considered to be different versions of a core nuclear localization signal, NLS. Core NLSs are present in nearly all nuclear proteins and absent from nearly all "nonassociated" cytoplasmic proteins that have been investigated. We suggest that the few ( -10%) protein factors lacking a typical NLS core peptide may enter the nucleus via their strong crosscomplexation with their protein factor partners that possess a core NLS. Those cytoplasmic proteins found to possess a NLS-like peptide are either tightly associated with cell membrane proteins or are integral components of large cytoplasmic protein complexes. On the other hand, some versions of core NLSs are found in many cell membrane proteins and secreted proteins. It is hypothesized that in these cases the N-terminal hydrophobic signal peptide of extracellular proteins and the internal hydrophobic domains of transmembrane proteins are stronger determinants for their subcellular localization. The position of core NLSs among homologous nuclear proteins may or may not be conserved; however, if lost from an homolgous site it appears elsewhere in the protein.This search provides a set of rules to our understanding of the nature of core nuclear localization signals: (1 ) Core NLS are proposed to consist most frequently of an hexapeptide with 4 arginines and lysines; ( 2 ) aspartic and glutamic acid residues as well as bulky amino acids (F, Y, W) need not to be present in this hexapeptide; (3) acidic residues and proline or glycine that break the a-helix are frequently in the flanking region of this hexapeptide stretch; (4) hydrophobic residues ought not to be present in the core NLS flanking region allowing for the NLS to be exposed on the protein. In this study we attempt to classify putative core NLS from a wealth of nuclear protein transcription factors from diverse species into several categories, and we propose additional core NLS structures yet to be experimentally verified. Key words: pore complex, transporter proteins, transcription factors, nuclear localization, nuclear proteins, basic region, cytoplasmic proteins, membrane proteins, c-Myc, c-Jun, NF-KB The nuclear envelope effectively separates transcription of genes from translation of their mRNA into proteins and allows proteins destined to function in the nucleus to pass selectively through the lumen of the nuclear pores [reviewed by Newport and Forbes, 1987; Boulikas, 19871. Pore complexes are anchored to the double nuclear membrane via the transmembrane glycoprotein gp210 [Wozniak et al., 19891 and with the aqueous channel that has an effective diameter of approximately 10 nm allow small proteins with a molecular weight inferior ~~ Abbreviations: ER, endoplasmic reticulum; aa, amino acid(s); NLS, nuclear localization signal.

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“…Experimental evidence also indicates the existence of NBPs that are involved in nuclear localization of proteins containing an NLS (20). All of the NBPs that have been described to date are of human, rat, or yeast origin, and the degree of sequence conservation is uncertain, because only yeast and rat NBP sequences have been reported (9,12).…”

Section: Conclusion and Future Prospectsmentioning

confidence: 99%

Nuclear Targeting in Plants

Raikhel¹

1992

Plant Physiol.

201

138

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The nucleus is the site of highly active two-way macromolecular traffic between the nucleoplasm and the cytoplasm. Nuclear import and export must be highly specific processes because the content of the nucleus is distinguished compared to the cytoplasm. This is rather amazing, considering that the nuclear envelope dissolves during mitosis of animal and plant cells, necessitating reassembly of all nuclear components and reentry of nuclear proteins into the nucleus. In addition, many basic cellular processes, such as gene transcription and cell division, clearly require proper nuclear localization of regulatory and housekeeping proteins. Furthermore, experimental evidence indicates the existence of receptors and other cellular factors that mediate nuclear transport. Nuclear transport, although extensively studied in animal and lower eukaryotic systems (3, 20), has only recently been addressed in higher plants (1,2,5,7,8,15,(24)(25)(26).This attention to protein and nucleic acid transport into the nucleus in plants was stimulated not only by a need to understand basic cell biology, but also by the desire to modulate or regulate the expression of genes via genetic engineering.The nucleus (Fig. 1) is surrounded by the nuclear envelope, which includes the inner and outer nuclear membranes and, between them, the perinuclear space. The outer nuclear membrane is contiguous with the rough ER, and its outer surface is generally studded with ribosomes. Underlying the inner nuclear membrane is the nuclear lamina, which is composed of a network of filamentous proteins. Unlike other organelles, the nuclear envelope contains NPC2, the major sites of bidirectional protein and nucleic acid traffic. Though understood on a structural level, knowledge of the biochemistry behind the NPC is limited. Only a few proteins associated with the NPC in animal systems have been identified (3); however, their actual involvement in nuclear import has not been demonstrated.Structurally, the NPC traverses the double membrane, bringing the lipid bilayers of the inner and outer membranes together around the margins of each pore. The NPC consists of eight large protein granules arranged in a circle with a large central granule or transporter that is thought to control active nucleocytoplasmic transport of large molecules (6). In

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The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs.

Cited by 171 publications

References 61 publications

An abundant nucleolar phosphoprotein is associated with ribosomal DNA in Tetrahymena macronuclei.

An abundant nucleolar phosphoprotein is associated with ribosomal DNA in Tetrahymena macronuclei.

Putative nuclear localization signals (NLS) in protein transcription factors

Nuclear Targeting in Plants

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