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Comparative Analysis of the Amino Terminus Region of Twist1 and Twist2 Proteins
Author(s) -
Rodriguez Yacidzohara,
GonzálezMendez Ricardo,
Cadilla Carmen
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.lb109
Subject(s) - biology , functional divergence , genetics , n terminus , gene , phylogenetic tree , sequence alignment , sequence analysis , gene duplication , peptide sequence , conserved sequence , c terminus , protein domain , vertebrate , computational biology , amino acid , gene family , genome
Twist proteins belong to the basic helix‐loop‐helix (bHLH) family of multifunctional transcriptional factors. ADD1, RunX2 and MEF2 have been shown to interact with TWIST2 in studies that suggest there are other elements or domains, besides the common bHLH, involved in these protein‐protein interactions. There have been attempts to characterize the roles of their N‐terminus, bHLH, and C‐terminus in protein‐protein interactions, more focus is needed at the N‐terminus. We analyzed the conservation of the N‐terminal region of different vertebrate Twist proteins by sequence comparison and motif analysis. We found two putative de novo motifs (SSSPVSP and SEEE), specifically in mammalian sequences. Mammalian Twist1 sequences contain two, already described, glycine rich motifs not present in Twist2 mammalian sequences or other vertebrate species. Disordered domain analysis and secondary structure prediction demonstrated that both the N‐ and C‐terminus are found in a disordered/flexible region. We investigated the origin and evolution of Twist proteins by phylogenetic analysis. First, a gene duplication event occurred to produce the two Twist paralogs, Twist1 being evolved first. Second, Twist2 vertebrate proteins seem to have a higher rate of sequence divergence when compared to Twist1 mammals since they do not contain the two additional glycine‐rich regions. Our study determined the relationship of Twist1 and Twist2 paralogs among mammals in vertebrates. Sequence conservation and diversity in the N‐terminus of mammalian Twist proteins provides a rationale for studies of the role of the N‐terminus in protein‐protein interactions. This research was supported through NIH grants T36GM008789 and P41 RR06009.