Evolutionary Dynamics

Evolutionary Analysis of Low Complexity Regions

 

Dr. Pablo Mier Muñoz

Researcher

SUMMARY


 

Visit the page of the LCE group for more information.

Low Complexity Regions (LCRs) are proteins regions where the frequency distribution of amino acids deviates from the common amino acid usage. Residues in LCRs have been estimated to represent 20% and 8% of all known sequences of eukaryotes and prokaryotes, respectively. In the definition of LCRs, multiple concepts related to sequence composition, periodicity and structure have been used. Regarding amino acid composition, while there is a general notion that LCRs in proteins should have an excess of one or a few types of amino acid residues, there is no consensus about which metrics are the most appropriate. Additionally, the concept of LCR is intermingled with the concept of sequence repeats. Repeats are inevitably associated with LCRs, since shorter repeats result in regions with lower amino acid diversity.

Homorepeats, polyX or amino acid repeats, are protein motifs defined as consecutive runs of a single residue. They are the simplest LCRs and rely on a highly localized abundance of an amino acid. Any amino acid can form them, although some polyX are much more abundant than others (which also depends on the species taxonomy). They are associated with multiple functionalities, from aiding protein localization to mediating protein–protein interactions. Many homorepeats have not been functionally characterized yet, despite their high abundance in eukaryotes. This makes them an interesting protein motif for a post-sequencing step in terms of proteome annotation.

Five relevant publications


 

  • Schumbera E+, Mier P+, Andrade-Navarro MA*. Phase separating Rho: a widespread regulatory function of disordered regions in proteins revealed in bacteria. Signal Transduction and Targeted Therapy 8(2023), 253. PMID: 37344523.
  • Mier P*, Paladin L, Tamana S, Petrosian S, Hajdu-Soltész B, Urbanek A, Gruca A, Plewczynski D, Grynberg M, Bernadó P, Gáspári Z, Ouzounis C, Promponas VJ, Kajava AV, Hancock JM, Tosatto SCE, Dosztanyi Z, Andrade-Navarro MA. Disentangling the complexity of low complexity proteins. Brief Bioinform 21(2020), 458-472. PMID: 30698641.
  • Jarnot P, Ziemska-Legiecka J, Dobson L, Merski M, Mier P, Andrade-Navarro M.A., Hancock J.M., Dosztanyi Z, Paladin L, Necci M, Piovesan D, Tosatto S.C.E., Promponas V.J., Grynberg M., Gruca A*. PlaToLoCo: the first web meta-server for visualization and annotation of low complexity regions in proteins. Nucleic Acids Res 48(2020), W77-W84. PMID: 32421769.
  • Mier P, Elena Real C, Urbanek A, Bernadó P, Andrade-Navarro MA*. The importance of definitions in the study of polyQ regions: a tale of thresholds, impurities and sequence context. Comput Struct Biotechnol J 18(2020), 306-313. PMID:32071707.
  • Tørresen OK, Star B, Mier P, Andrade-Navarro MA, Bateman A, Jarnot P, Gruca A, Grynberg M, Kajava AV, Promponas VJ, Anisimova M, Jakobsen KS, Linke D*. Tandem repeats lead to sequence assembly errors and impose multi-level challenges for genome and protein databases. Nucleic Acids Res 47(2019), 10994-11006. PMID: 31584084.

Complete list in Pubmed

Lab members & collaborators


 

Lab members

Beatriz Galindo

Researcher:

Dr. Pablo Mier

PhD student:

Nerea Blanco

Collaborators

Dr. Miguel Andrade-Navarro (Johannes Gutenberg University Mainz, Germany)

Dr. Pau Bernadó (Centre de Biochimie Structurale, France)

Dr. Aleksandra Gruca (Silesian University of Technology, Poland)

Dr. Marcin Grynberg (Institute of Biochemistry and Biophysics, Poland)

Dr. David Kreil (University of Natural Resources and Life Sciences Vienna, Austria)

Dr. Enrique Morett (Universidad Nacional Autonoma de Mexico, Mexico)