Identification of an unconventional nuclear localization signal in human ribosomal protein S2

Antoine, M; Reimers, K; Wirz, W; Gressner, A M; Mueller, R; Kiefer, P

doi:10.1016/j.bbrc.2005.07.069

Title: Identification of an unconventional nuclear localization signal in human ribosomal protein S2

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Abstract

Ribosomal proteins must be imported into the nucleus after being synthesized in the cytoplasm. Since the rpS2 amino acid sequence does not contain a typical nuclear localization signal, we used deletion mutant analysis and rpS2-{beta}-galactosidase chimeric proteins to identify the nuclear targeting domains in rpS2. Nuclear rpS2 is strictly localized in the nucleoplasm and is not targeted to the nucleoli. Subcellular localization analysis of deletion mutants of rpS2-{beta}-galactosidase chimeras identified a central domain comprising 72 amino acids which is necessary and sufficient to target the chimeric {beta}-galactosidase to the nucleus. The nuclear targeting domain shares no significant similarity to already characterized nuclear localization signals in ribosomal proteins or other nuclear proteins. Although a Nup153 fragment containing the importin{beta} binding site fused to VP22 blocks nuclear import of rpS2-{beta}-galactosidase fusion proteins, nuclear uptake of rpS2 could be mediated by several import receptors since it binds to importin{alpha}/{beta} and transportin.

Authors:

Antoine, M ^[1]; Reimers, K ^[2]; Wirz, W ^[1]; Gressner, A M ^[1]; Mueller, R ^[1]; Kiefer, P ^[1]

Institute of Clinical Chemistry and Pathobiochemistry, RWTH Aachen, (Germany)
Department for Plastic, Hand and Reconstructive Surgery, Medical School Hannover, Podbielskistrasse 380, D-30659 Hannover, (Germany)

Publication Date:: Fri Sep 16 00:00:00 EDT 2005

OSTI Identifier:: 20710968

Resource Type:: Journal Article

Journal Name:: Biochemical and Biophysical Research Communications

Additional Journal Information:: Journal Volume: 335; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2005.07.069; PII: S0006-291X(05)01514-7; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; AMINO ACID SEQUENCE; AMINO ACIDS; CHIMERAS; CYTOPLASM; GALACTOSIDASE; IMPORTS; MUTANTS; NUCLEOLI; RECEPTORS

Citation Formats


                    Antoine, M, Reimers, K, Wirz, W, Gressner, A M, Mueller, R, and Kiefer, P. Identification of an unconventional nuclear localization signal in human ribosomal protein S2.  United States: N. p., 2005. 
        Web.  doi:10.1016/j.bbrc.2005.07.069.

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                    Antoine, M, Reimers, K, Wirz, W, Gressner, A M, Mueller, R, & Kiefer, P. Identification of an unconventional nuclear localization signal in human ribosomal protein S2.  United States.  https://doi.org/10.1016/j.bbrc.2005.07.069

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                    Antoine, M, Reimers, K, Wirz, W, Gressner, A M, Mueller, R, and Kiefer, P. 2005.  
        "Identification of an unconventional nuclear localization signal in human ribosomal protein S2".  United States.  https://doi.org/10.1016/j.bbrc.2005.07.069.

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@article{osti_20710968,

  title        = {Identification of an unconventional nuclear localization signal in human ribosomal protein S2},

  author       = {Antoine, M and Reimers, K and Wirz, W and Gressner, A M and Mueller, R and Kiefer, P},

  abstractNote = {Ribosomal proteins must be imported into the nucleus after being synthesized in the cytoplasm. Since the rpS2 amino acid sequence does not contain a typical nuclear localization signal, we used deletion mutant analysis and rpS2-{beta}-galactosidase chimeric proteins to identify the nuclear targeting domains in rpS2. Nuclear rpS2 is strictly localized in the nucleoplasm and is not targeted to the nucleoli. Subcellular localization analysis of deletion mutants of rpS2-{beta}-galactosidase chimeras identified a central domain comprising 72 amino acids which is necessary and sufficient to target the chimeric {beta}-galactosidase to the nucleus. The nuclear targeting domain shares no significant similarity to already characterized nuclear localization signals in ribosomal proteins or other nuclear proteins. Although a Nup153 fragment containing the importin{beta} binding site fused to VP22 blocks nuclear import of rpS2-{beta}-galactosidase fusion proteins, nuclear uptake of rpS2 could be mediated by several import receptors since it binds to importin{alpha}/{beta} and transportin.},

  doi          = {10.1016/j.bbrc.2005.07.069},

  url          = {https://www.osti.gov/biblio/20710968},
  journal      = {Biochemical and Biophysical Research Communications},

  issn         = {0006-291X},

  number       = 1,

  volume       = 335,

  place        = {United States},

  year         = {Fri Sep 16 00:00:00 EDT 2005},

  month        = {Fri Sep 16 00:00:00 EDT 2005}

}

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