Intrinsic protein disorder in complete genomes
- PMID: 11700597
Intrinsic protein disorder in complete genomes
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.
Similar articles
-
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life.J Biomol Struct Dyn. 2012;30(2):137-49. doi: 10.1080/07391102.2012.675145. J Biomol Struct Dyn. 2012. PMID: 22702725
-
Intrinsic disorder of the extracellular matrix.Mol Biosyst. 2011 Dec;7(12):3353-65. doi: 10.1039/c1mb05316g. Epub 2011 Oct 19. Mol Biosyst. 2011. PMID: 22009114
-
Unexpected features of the dark proteome.Proc Natl Acad Sci U S A. 2015 Dec 29;112(52):15898-903. doi: 10.1073/pnas.1508380112. Epub 2015 Nov 17. Proc Natl Acad Sci U S A. 2015. PMID: 26578815 Free PMC article.
-
Intrinsically disordered protein.J Mol Graph Model. 2001;19(1):26-59. doi: 10.1016/s1093-3263(00)00138-8. J Mol Graph Model. 2001. PMID: 11381529 Review.
-
Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins.Brief Bioinform. 2010 Mar;11(2):225-43. doi: 10.1093/bib/bbp061. Epub 2009 Dec 10. Brief Bioinform. 2010. PMID: 20007729 Review.
Cited by
-
Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013. PeerJ. 2013. PMID: 23638354 Free PMC article.
-
Comparison of Secondary Structure Formation Using 10 Different Force Fields in Microsecond Molecular Dynamics Simulations.J Chem Theory Comput. 2012 Aug 14;8(8):2725-2740. doi: 10.1021/ct300323g. Epub 2012 Jun 19. J Chem Theory Comput. 2012. PMID: 22904695 Free PMC article.
-
The MDMX Acidic Domain Uses Allovalency to Bind Both p53 and MDMX.J Mol Biol. 2022 Nov 30;434(22):167844. doi: 10.1016/j.jmb.2022.167844. Epub 2022 Sep 29. J Mol Biol. 2022. PMID: 36181774 Free PMC article.
-
The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions.J Biol Chem. 2012 Nov 16;287(47):39982-91. doi: 10.1074/jbc.M112.414292. Epub 2012 Oct 1. J Biol Chem. 2012. PMID: 23027878 Free PMC article.
-
Predicting mostly disordered proteins by using structure-unknown protein data.BMC Bioinformatics. 2007 Mar 6;8:78. doi: 10.1186/1471-2105-8-78. BMC Bioinformatics. 2007. PMID: 17338828 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Other Literature Sources
Molecular Biology Databases