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Hox functional diversity: Novel insights from flexible motif folding and plastic protein interaction
Author(s) -
OrtizLombardia Miguel,
Foos Nicolas,
MaurelZaffran Corinne,
Saurin Andrew J.,
Graba Yacine
Publication year - 2017
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201600246
Subject(s) - hox gene , biology , computational biology , evolutionary biology , homeobox , functional diversity , transcription factor , context (archaeology) , protein–protein interaction , protein folding , folding (dsp implementation) , genetics , gene , microbiology and biotechnology , ecology , paleontology , engineering , electrical engineering
How the formidable diversity of forms emerges from developmental and evolutionary processes is one of the most fascinating questions in biology. The homeodomain‐containing Hox proteins were recognized early on as major actors in diversifying animal body plans. The molecular mechanisms underlying how this transcription factor family controls a large array of context‐ and cell‐specific biological functions is, however, still poorly understood. Clues to functional diversity have emerged from studies exploring how Hox protein activity is controlled through interactions with PBC class proteins, also evolutionary conserved HD‐containing proteins. Recent structural data and molecular dynamic simulations add further mechanistic insights into Hox protein mode of action, suggesting that flexible folding of protein motifs allows for plastic protein interaction. As we discuss in this review, these findings define a novel type of Hox‐PBC interaction, weak and dynamic instead of strong and static, hence providing novel clues to understanding Hox transcriptional specificity and diversity.