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A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome

Intrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional... Full description

Journal Title: Cellular and Molecular Life Sciences 2013-08-13, Vol.71 (8), p.1477-1504
Main Author: Peng, Zhenling
Other Authors: Oldfield, Christopher J , Xue, Bin , Mizianty, Marcin J , Dunker, A. Keith , Kurgan, Lukasz , Uversky, Vladimir N
Format: Electronic Article Electronic Article
Language: English
Subjects:
RNA
Publisher: Basel: Springer Basel
ID: ISSN: 1420-682X
Link: https://www.ncbi.nlm.nih.gov/pubmed/23942625
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title: A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome
format: Article
creator:
  • Peng, Zhenling
  • Oldfield, Christopher J
  • Xue, Bin
  • Mizianty, Marcin J
  • Dunker, A. Keith
  • Kurgan, Lukasz
  • Uversky, Vladimir N
subjects:
  • Alzheimer's disease
  • Amino Acids - analysis
  • Analysis
  • Archaea - genetics
  • Bacteria - genetics
  • Binding proteins
  • Biochemistry
  • Bioinformatics
  • Biomedical and Life Sciences
  • Biomedicine
  • Cell Biology
  • Computational Biology
  • Conserved Sequence - genetics
  • Databases, Protein
  • Electric properties
  • Eukaryota - genetics
  • Evolution, Molecular
  • general
  • Intrinsically disordered protein
  • Intrinsically Disordered Proteins - genetics
  • Intrinsically Disordered Proteins - metabolism
  • Life Sciences
  • Models, Molecular
  • Molecular biology
  • Moonlighting protein
  • Protein binding
  • Protein Conformation
  • Protein Structure, Tertiary - genetics
  • Proteins
  • Protein–protein interaction
  • Protein–RNA interaction
  • Research Article
  • Ribonucleic acid
  • Ribosomal proteins
  • Ribosomal Proteins - genetics
  • Ribosomal Proteins - metabolism
  • Ribosomes - metabolism
  • RNA
  • RNA-Binding Proteins - genetics
  • RNA-Binding Proteins - metabolism
  • Species Specificity
ispartof: Cellular and Molecular Life Sciences, 2013-08-13, Vol.71 (8), p.1477-1504
description: Intrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein–protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.
language: eng
source:
identifier: ISSN: 1420-682X
fulltext: no_fulltext
issn:
  • 1420-682X
  • 1420-9071
url: Link


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titleA creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome
creatorPeng, Zhenling ; Oldfield, Christopher J ; Xue, Bin ; Mizianty, Marcin J ; Dunker, A. Keith ; Kurgan, Lukasz ; Uversky, Vladimir N
creatorcontribPeng, Zhenling ; Oldfield, Christopher J ; Xue, Bin ; Mizianty, Marcin J ; Dunker, A. Keith ; Kurgan, Lukasz ; Uversky, Vladimir N
descriptionIntrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein–protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.
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languageeng
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subjectAlzheimer's disease ; Amino Acids - analysis ; Analysis ; Archaea - genetics ; Bacteria - genetics ; Binding proteins ; Biochemistry ; Bioinformatics ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Computational Biology ; Conserved Sequence - genetics ; Databases, Protein ; Electric properties ; Eukaryota - genetics ; Evolution, Molecular ; general ; Intrinsically disordered protein ; Intrinsically Disordered Proteins - genetics ; Intrinsically Disordered Proteins - metabolism ; Life Sciences ; Models, Molecular ; Molecular biology ; Moonlighting protein ; Protein binding ; Protein Conformation ; Protein Structure, Tertiary - genetics ; Proteins ; Protein–protein interaction ; Protein–RNA interaction ; Research Article ; Ribonucleic acid ; Ribosomal proteins ; Ribosomal Proteins - genetics ; Ribosomal Proteins - metabolism ; Ribosomes - metabolism ; RNA ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Species Specificity
ispartofCellular and Molecular Life Sciences, 2013-08-13, Vol.71 (8), p.1477-1504
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descriptionIntrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein–protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.
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3Archaea - genetics
4Bacteria - genetics
5Binding proteins
6Biochemistry
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10Cell Biology
11Computational Biology
12Conserved Sequence - genetics
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26Protein Conformation
27Protein Structure, Tertiary - genetics
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29Protein–protein interaction
30Protein–RNA interaction
31Research Article
32Ribonucleic acid
33Ribosomal proteins
34Ribosomal Proteins - genetics
35Ribosomal Proteins - metabolism
36Ribosomes - metabolism
37RNA
38RNA-Binding Proteins - genetics
39RNA-Binding Proteins - metabolism
40Species Specificity
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titleA creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome
authorPeng, Zhenling ; Oldfield, Christopher J ; Xue, Bin ; Mizianty, Marcin J ; Dunker, A. Keith ; Kurgan, Lukasz ; Uversky, Vladimir N
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6Biochemistry
7Bioinformatics
8Biomedical and Life Sciences
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38RNA-Binding Proteins - genetics
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abstractIntrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein–protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.
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