A new census of protein tandem repeats and their relationship with intrinsic disorder room

Delucchi, Matteo

doi:10.3390/genes11040407

Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-20159

Publication type:	Conference poster
Type of review:	No review
Title:	A new census of protein tandem repeats and their relationship with intrinsic disorder room
Authors:	Delucchi, Matteo
et. al:	No
DOI:	10.3390/genes11040407 10.21256/zhaw-20159
Published in:	Genes
Volume(Issue):	11
Issue:	4
Page(s):	407
Conference details:	SIB Days 2020, virtual conference, 8-10 June 2020
Issue Date:	9-Jun-2020
Publisher / Ed. Institution:	ZHAW Zürcher Hochschule für Angewandte Wissenschaften
Language:	English
Subjects:	Tandem repeat; Homorepeat; Domain repeat; Protein repeat; Repeat prediction; Intrinsic disorder; Protein function; Swiss-Prot
Subject (DDC):	572: Biochemistry
Abstract:	Protein tandem repeats (TRs) are often associated with immunity-related functions and diseases. Since that last census of protein TRs in 1999, the number of curated proteins increased more than seven-fold and new TR prediction methods were published. TRs appear to be enriched with intrinsic disorder and vice versa. The significance and the biological reasons for this association are unknown. Here, we characterize protein TRs across all kingdoms of life and their overlap with intrinsic disorder in unprecedented detail. Using state-of-the-art prediction methods, we estimate that 50.9% of proteins contain at least one TR, often located at the sequence flanks. Positive linear correlation between the proportion of TRs and the protein length was observed universally, with Eukaryotes in general having more TRs, but when the difference in length is taken into account the difference is quite small. TRs were enriched with disorder promoting amino acids and were inside intrinsically disordered regions. Many such TRs were homorepeats. Our results support that TRs mostly originate by duplication and are involved in essential functions such as transcription processes, structural organization, electron transport and iron-binding. In viruses, TRs are found in proteins essential for virulence.
URI:	https://digitalcollection.zhaw.ch/handle/11475/20159
Fulltext version:	Published version
License (according to publishing contract):	CC BY 4.0: Attribution 4.0 International
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Computational Life Sciences (ICLS)
Published as part of the ZHAW project:	EU MSCA REFRACT: Repeat protein Function, Refinement, Annotation and Classification of Topologies
Appears in collections:	Publikationen Life Sciences und Facility Management

Files in This Item:

File	Description	Size	Format
2020_Delucchi_SIB-Days_Poster.png		3.86 MB	image/png	View/Open

Show full item record

Delucchi, M. (2020). A new census of protein tandem repeats and their relationship with intrinsic disorder room [Conference poster]. Genes, 11(4), 407. https://doi.org/10.3390/genes11040407

Delucchi, M. (2020) ‘A new census of protein tandem repeats and their relationship with intrinsic disorder room’, in Genes. ZHAW Zürcher Hochschule für Angewandte Wissenschaften, p. 407. Available at: https://doi.org/10.3390/genes11040407.

M. Delucchi, “A new census of protein tandem repeats and their relationship with intrinsic disorder room,” in Genes, Jun. 2020, vol. 11, no. 4, p. 407. doi: 10.3390/genes11040407.

DELUCCHI, Matteo, 2020. A new census of protein tandem repeats and their relationship with intrinsic disorder room. In: Genes. Conference poster. ZHAW Zürcher Hochschule für Angewandte Wissenschaften. 9 Juni 2020. S. 407

Delucchi, Matteo. 2020. “A New Census of Protein Tandem Repeats and Their Relationship with Intrinsic Disorder Room.” Conference poster. In Genes, 11:407. ZHAW Zürcher Hochschule für Angewandte Wissenschaften. https://doi.org/10.3390/genes11040407.

Delucchi, Matteo. “A New Census of Protein Tandem Repeats and Their Relationship with Intrinsic Disorder Room.” Genes, vol. 11, no. 4, ZHAW Zürcher Hochschule für Angewandte Wissenschaften, 2020, p. 407, https://doi.org/10.3390/genes11040407.