Structural Disorder in Eukaryotes

被引:146
作者
Pancsa, Rita [1 ]
Tompa, Peter [1 ,2 ]
机构
[1] Vrije Univ Brussel VIB, Dept Biol Struct, B-1050 Brussels, Belgium
[2] Hungarian Acad Sci, Inst Enzymol, Budapest, Hungary
来源
PLOS ONE | 2012年 / 7卷 / 04期
关键词
INTRINSICALLY UNSTRUCTURED PROTEINS; AMINO-ACID-COMPOSITION; PREDICTION; REGIONS; EVOLUTION; SCAFFOLD; DOMAINS;
D O I
10.1371/journal.pone.0034687
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Based on early bioinformatic studies on a handful of species, the frequency of structural disorder of proteins is generally thought to be much higher in eukaryotes than in prokaryotes. To refine this view, we present here a comparative prediction study and analysis of 194 fully described eukaryotic proteomes and 87 reference prokaryotes for structural disorder. We found that structural disorder does distinguish eukaryotes from prokaryotes, but its frequency spans a very wide range in the two superkingdoms that largely overlap. The number of disordered binding regions and different Pfam domain types also contribute to distinguish eukaryotes from prokaryotes. Unexpectedly, the highest levels - and highest variability - of predicted disorder is found in protists, i.e. single-celled eukaryotes, often surpassing more complex eukaryote organisms, plants and animals. This trend contrasts with that of the number of domain types, which increases rather monotonously toward more complex organisms. The level of structural disorder appears to be strongly correlated with lifestyle, because some obligate intracellular parasites and endosymbionts have the lowest levels, whereas host-changing parasites have the highest level of predicted disorder. We conclude that protists have been the evolutionary hot-bed of experimentation with structural disorder, in a period when structural disorder was actively invented and the major functional classes of disordered proteins established.
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页数:10
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共 54 条
[1]   Ongoing and future developments at the Universal Protein Resource [J].
Apweiler, Rolf ;
Martin, Maria Jesus ;
O'Donovan, Claire ;
Magrane, Michele ;
Alam-Faruque, Yasmin ;
Antunes, Ricardo ;
Barrell, Daniel ;
Bely, Benoit ;
Bingley, Mark ;
Binns, David ;
Bower, Lawrence ;
Browne, Paul ;
Chan, Wei Mun ;
Dimmer, Emily ;
Eberhardt, Ruth ;
Fazzini, Francesco ;
Fedotov, Alexander ;
Foulger, Rebecca ;
Garavelli, John ;
Castro, Leyla Garcia ;
Huntley, Rachael ;
Jacobsen, Julius ;
Kleen, Michael ;
Laiho, Kati ;
Legge, Duncan ;
Lin, Quan ;
Liu, Wudong ;
Luo, Jie ;
Orchard, Sandra ;
Patient, Samuel ;
Pichler, Klemens ;
Poggioli, Diego ;
Pontikos, Nikolas ;
Pruess, Manuela ;
Rosanoff, Steven ;
Sawford, Tony ;
Sehra, Harminder ;
Turner, Edward ;
Corbett, Matt ;
Donnelly, Mike ;
van Rensburg, Pieter ;
Xenarios, Ioannis ;
Bougueleret, Lydie ;
Auchincloss, Andrea ;
Argoud-Puy, Ghislaine ;
Axelsen, Kristian ;
Bairoch, Amos ;
Baratin, Delphine ;
Blatter, Marie-Claude ;
Boeckmann, Brigitte .
NUCLEIC ACIDS RESEARCH, 2011, 39 :D214-D219
[2]   High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1 [J].
Balazs, Annamaria ;
Csizmok, Veronika ;
Buday, Laszlo ;
Rakacs, Marianna ;
Kiss, Robert ;
Bokor, Monika ;
Udupa, Roopesh ;
Tompa, Kalman ;
Tompa, Peter .
FEBS JOURNAL, 2009, 276 (14) :3744-3756
[3]   Evolution and disorder [J].
Brown, Celeste J. ;
Johnson, Audra K. ;
Dunker, A. Keith ;
Daughdrill, Gary W. .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2011, 21 (03) :441-446
[4]   Reduction in Structural Disorder and Functional Complexity in the Thermal Adaptation of Prokaryotes [J].
Burra, Prasad V. ;
Kalmar, Lajos ;
Tompa, Peter .
PLOS ONE, 2010, 5 (08)
[5]   Primary contact sites in intrinsically unstructured proteins:: The case of calpastatin and microtubule-associated protein 2 [J].
Csizmók, V ;
Bokor, M ;
Bánki, P ;
Klement, T ;
Medzihradszky, KF ;
Friedrich, P ;
Tompa, K ;
Tompa, P .
BIOCHEMISTRY, 2005, 44 (10) :3955-3964
[6]   Natively unfolded domains in endocytosis: hooks, lines and linkers [J].
Dafforn, TR ;
Smith, CJI .
EMBO REPORTS, 2004, 5 (11) :1046-1052
[7]   How viruses hijack cell regulation [J].
Davey, Norman E. ;
Trave, Gilles ;
Gibson, Toby J. .
TRENDS IN BIOCHEMICAL SCIENCES, 2011, 36 (03) :159-169
[8]   Understanding eukaryotic linear motifs and their role in cell signaling and regulation [J].
Diella, Francesca ;
Haslam, Niall ;
Chica, Claudia ;
Budd, Aidan ;
Michael, Sushama ;
Brown, Nigel P. ;
Trave, Gilles ;
Gibson, Toby J. .
FRONTIERS IN BIOSCIENCE-LANDMARK, 2008, 13 :6580-6603
[9]   IUPred:: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content [J].
Dosztányi, Z ;
Csizmok, V ;
Tompa, P ;
Simon, I .
BIOINFORMATICS, 2005, 21 (16) :3433-3434
[10]   The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins [J].
Dosztányi, Z ;
Csizmók, V ;
Tompa, P ;
Simon, I .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (04) :827-839