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CAST is used for detecting (and subsequently masking) low-complexity regions (LCRs) in protein sequences.
Analysis of the 2-Mb region susceptible to duplications identified proximal-specific repeats and distal LCRs in addition to the previously reported ones, suggesting that the unique genomic architecture may have a role in nonrecurrent rearrangements by promoting instability.
By species we obtained 487 LCRs in human, 479 LCRs in mouse, 367 LCRs in chicken, 494 LCRs in zebrafish and 167 LCRs in C.intestinalis.
We classified 1,104 LCRs in different age groups.
For example, many low copy repeats (LCRs) in mammalian genomes are induced by segmental duplications [ 10].
In patient 2, three of the eight breakpoints were associated with LCRs in proximal 17p.
A Gene Ontology term enrichment test detected known associations such as an overrepresentation of serine and arginine (SR -rich LCRSR -richteins invoLCRs in RNA sproteins[ 22], and alaninvolved glutamine-RNAh LCRsplicingnscription factors [ 5, 13].
Our results show that LCRs are preferentially located towards sequence extremities, and that proteins with LCRs in their sequence extremities have more protein binding partners than proteins with LCRs in their central regions.
The study presented here is the first attempt to follow the evolutionary history of a large set of LCRs in order to obtain novel insights into the role of LCRs in protein evolution.
Low-complexity regions (LCRs) in protein sequences are regions containing little diversity in their amino acid composition.
We have performed the first large-scale study on the evolutionary dynamics of LCRs in protein families.
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Justyna Jupowicz-Kozak
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