RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153

Christian Dimaano, Jennifer R. Ball, Amy J. Prunuske, Katharine S. Ullman

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Traffic between the nucleus and cytoplasm takes place through a macromolecular structure termed the nuclear pore complex. To understand how the vital process of nucleocytoplasmic transport occurs, the contribution of individual pore proteins must be elucidated. One such protein, the nucleoporin Nup153, is localized to the nuclear basket of the pore complex and has been shown to be a central component of the nuclear transport machinery. Perturbation of Nup153 function was demonstrated previously to block the export of several classes of RNA cargo. Moreover, these studies also showed that Nup153 can stably associate with RNA in vitro. In this study, we have mapped a domain within Nup153, encompassing amino acids 250-400 in human Nup153, that is responsible for RNA association. After cloning this region of Xenopus Nup153, we performed a cross-species analysis. Despite variation in sequence conservation between Drosophila, Xenopus, and human, this domain of Nup153 displayed robust RNA binding activity in each case, indicating that this property is a hallmark feature of Nup153 and pointing toward a subset of amino acid residues that are key to conferring this ability. We have further determined that a recombinant fragment of Nup153 can bind directly to RNA and that this fragment can interact with endogenous RNA targets. Our findings identify a functionally conserved domain in Nup153 and suggest a role for RNA binding in Nup153 function at the nuclear pore.

Original languageEnglish (US)
Pages (from-to)45349-45357
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number48
DOIs
StatePublished - Nov 30 2001

Fingerprint

Nuclear Pore
Porins
Nuclear Proteins
RNA
Cell Nucleus Active Transport
Xenopus
Nuclear Pore Complex Proteins
Amino Acids
Cloning
Drosophila
Machinery
Organism Cloning
Conservation
Cytoplasm

Cite this

RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153. / Dimaano, Christian; Ball, Jennifer R.; Prunuske, Amy J.; Ullman, Katharine S.

In: Journal of Biological Chemistry, Vol. 276, No. 48, 30.11.2001, p. 45349-45357.

Research output: Contribution to journalArticle

Dimaano, Christian ; Ball, Jennifer R. ; Prunuske, Amy J. ; Ullman, Katharine S. / RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 48. pp. 45349-45357.
@article{a3029fb30a554cc4a0c8f3d4527d12cf,
title = "RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153",
abstract = "Traffic between the nucleus and cytoplasm takes place through a macromolecular structure termed the nuclear pore complex. To understand how the vital process of nucleocytoplasmic transport occurs, the contribution of individual pore proteins must be elucidated. One such protein, the nucleoporin Nup153, is localized to the nuclear basket of the pore complex and has been shown to be a central component of the nuclear transport machinery. Perturbation of Nup153 function was demonstrated previously to block the export of several classes of RNA cargo. Moreover, these studies also showed that Nup153 can stably associate with RNA in vitro. In this study, we have mapped a domain within Nup153, encompassing amino acids 250-400 in human Nup153, that is responsible for RNA association. After cloning this region of Xenopus Nup153, we performed a cross-species analysis. Despite variation in sequence conservation between Drosophila, Xenopus, and human, this domain of Nup153 displayed robust RNA binding activity in each case, indicating that this property is a hallmark feature of Nup153 and pointing toward a subset of amino acid residues that are key to conferring this ability. We have further determined that a recombinant fragment of Nup153 can bind directly to RNA and that this fragment can interact with endogenous RNA targets. Our findings identify a functionally conserved domain in Nup153 and suggest a role for RNA binding in Nup153 function at the nuclear pore.",
author = "Christian Dimaano and Ball, {Jennifer R.} and Prunuske, {Amy J.} and Ullman, {Katharine S.}",
year = "2001",
month = "11",
day = "30",
doi = "10.1074/jbc.M102592200",
language = "English (US)",
volume = "276",
pages = "45349--45357",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "48",

}

TY - JOUR

T1 - RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153

AU - Dimaano, Christian

AU - Ball, Jennifer R.

AU - Prunuske, Amy J.

AU - Ullman, Katharine S.

PY - 2001/11/30

Y1 - 2001/11/30

N2 - Traffic between the nucleus and cytoplasm takes place through a macromolecular structure termed the nuclear pore complex. To understand how the vital process of nucleocytoplasmic transport occurs, the contribution of individual pore proteins must be elucidated. One such protein, the nucleoporin Nup153, is localized to the nuclear basket of the pore complex and has been shown to be a central component of the nuclear transport machinery. Perturbation of Nup153 function was demonstrated previously to block the export of several classes of RNA cargo. Moreover, these studies also showed that Nup153 can stably associate with RNA in vitro. In this study, we have mapped a domain within Nup153, encompassing amino acids 250-400 in human Nup153, that is responsible for RNA association. After cloning this region of Xenopus Nup153, we performed a cross-species analysis. Despite variation in sequence conservation between Drosophila, Xenopus, and human, this domain of Nup153 displayed robust RNA binding activity in each case, indicating that this property is a hallmark feature of Nup153 and pointing toward a subset of amino acid residues that are key to conferring this ability. We have further determined that a recombinant fragment of Nup153 can bind directly to RNA and that this fragment can interact with endogenous RNA targets. Our findings identify a functionally conserved domain in Nup153 and suggest a role for RNA binding in Nup153 function at the nuclear pore.

AB - Traffic between the nucleus and cytoplasm takes place through a macromolecular structure termed the nuclear pore complex. To understand how the vital process of nucleocytoplasmic transport occurs, the contribution of individual pore proteins must be elucidated. One such protein, the nucleoporin Nup153, is localized to the nuclear basket of the pore complex and has been shown to be a central component of the nuclear transport machinery. Perturbation of Nup153 function was demonstrated previously to block the export of several classes of RNA cargo. Moreover, these studies also showed that Nup153 can stably associate with RNA in vitro. In this study, we have mapped a domain within Nup153, encompassing amino acids 250-400 in human Nup153, that is responsible for RNA association. After cloning this region of Xenopus Nup153, we performed a cross-species analysis. Despite variation in sequence conservation between Drosophila, Xenopus, and human, this domain of Nup153 displayed robust RNA binding activity in each case, indicating that this property is a hallmark feature of Nup153 and pointing toward a subset of amino acid residues that are key to conferring this ability. We have further determined that a recombinant fragment of Nup153 can bind directly to RNA and that this fragment can interact with endogenous RNA targets. Our findings identify a functionally conserved domain in Nup153 and suggest a role for RNA binding in Nup153 function at the nuclear pore.

UR - http://www.scopus.com/inward/record.url?scp=0035977057&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035977057&partnerID=8YFLogxK

U2 - 10.1074/jbc.M102592200

DO - 10.1074/jbc.M102592200

M3 - Article

VL - 276

SP - 45349

EP - 45357

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 48

ER -