Literature DB >> 11700597

Intrinsic protein disorder in complete genomes.

A K Dunker1, Z Obradovic, P Romero, E C Garner, C J Brown.   

Abstract

Intrinsic protein disorder refers to segments or to whole proteins that fail to fold completely on their own. Here we predicted disorder on protein sequences from 34 genomes, including 22 bacteria, 7 archaea, and 5 eucaryotes. Predicted disordered segments > or = 50, > or = 40, and > or = 30 in length were determined as well as proteins estimated to be wholly disordered. The five eucaryotes were separated from bacteria and archaea by having the highest percentages of sequences predicted to have disordered segments > or = 50 in length: from 25% for Plasmodium to 41% for Drosophila. Estimates of wholly disordered proteins in the bacteria ranged from 1% to 8%, averaging to 3 +/- 2%, estimates in various archaea ranged from 2 to 11%, plus an apparently anomalous 18%, averaging to 7 +/- 5% that drops to 5 +/- 3% if the high value is discarded. Estimates in the 5 eucarya ranged from 3 to 17%. The putative wholly disordered proteins were often ribosomal proteins, but in addition about equal numbers were of known and unknown function. Overall, intrinsic disorder appears to be a common, with eucaryotes perhaps having a higher percentage of native disorder than archaea or bacteria.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11700597

Source DB:  PubMed          Journal:  Genome Inform Ser Workshop Genome Inform


  289 in total

1.  SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?

Authors:  K Moncoq; I Broutin; C T Craescu; P Vachette; A Ducruix; D Durand
Journal:  Biophys J       Date:  2004-10-01       Impact factor: 4.033

2.  Intrinsic disorder modulates protein self-assembly and aggregation.

Authors:  Alfonso De Simone; Craig Kitchen; Ann H Kwan; Margaret Sunde; Christopher M Dobson; Daan Frenkel
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-16       Impact factor: 11.205

Review 3.  Understanding protein non-folding.

Authors:  Vladimir N Uversky; A Keith Dunker
Journal:  Biochim Biophys Acta       Date:  2010-02-01

Review 4.  Oncogenic partnerships: EWS-FLI1 protein interactions initiate key pathways of Ewing's sarcoma.

Authors:  Hayriye V Erkizan; Vladimir N Uversky; Jeffrey A Toretsky
Journal:  Clin Cancer Res       Date:  2010-06-14       Impact factor: 12.531

5.  Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein.

Authors:  Alexander F Chin; Dmitri Toptygin; W Austin Elam; Travis P Schrank; Vincent J Hilser
Journal:  Biophys J       Date:  2016-01-19       Impact factor: 4.033

Review 6.  Selection on protein structure, interaction, and sequence.

Authors:  Peter B Chi; David A Liberles
Journal:  Protein Sci       Date:  2016-02-11       Impact factor: 6.725

7.  Mechanism of cell cycle entry mediated by the intrinsically disordered protein p27(Kip1).

Authors:  Li Ou; M Brett Waddell; Richard W Kriwacki
Journal:  ACS Chem Biol       Date:  2012-02-03       Impact factor: 5.100

Review 8.  The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein.

Authors:  Oleg Laptenko; David R Tong; James Manfredi; Carol Prives
Journal:  Trends Biochem Sci       Date:  2016-09-23       Impact factor: 13.807

Review 9.  Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.

Authors:  Deepa Balasubramaniam; Elizabeth A Komives
Journal:  Biochim Biophys Acta       Date:  2012-10-22

10.  Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins.

Authors:  Wei Ye; Dingjue Ji; Wei Wang; Ray Luo; Hai-Feng Chen
Journal:  J Chem Inf Model       Date:  2015-05-13       Impact factor: 4.956

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.