Identification of evolutionarily conserved amino acid residues in homeodomain of KNOX proteins for intercellular trafficking

Chen, H., Jackson, D., Kim, J. Y. (2014) Identification of evolutionarily conserved amino acid residues in homeodomain of KNOX proteins for intercellular trafficking. Plant Signaling and Behavior, 9 (2). ISSN 1559-2316

URL: http://www.ncbi.nlm.nih.gov/pubmed/24603432

Abstract

Maize KNOTTED (KN1) homeodomain (HD) protein is a well-known mobile transcription factor crucial for stem cell maintenance. Recent studies have revealed that the trihelical HD of KNOTTED1-like homeobox (KNOX) proteins is necessary and sufficient for selective cell-to-cell trafficking. Also, the efficient trafficking ability for HD is likely to be acquired during the evolution of early nonvascular land plants. Here, using the point-mutated HD of KN1 and SHOOT MERISTEMLESS (STM) in the trichome rescue system, together with molecular structure modeling, we have found the evolutionarily conserved amino acid residues, such as arginine in helix alpha1 and leucine in helix alpha3, which are essential for intercellular trafficking. Our studies provided important clues for the 3-dimensional protein structure required for cell-to-cell movement of non-cell-autonomous transcription factors.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > homeodomain protein
organism description > plant
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Jackson lab
Depositing User: Matt Covey
Date Deposited: 14 Mar 2014 15:25
Last Modified: 16 Mar 2015 19:03
PMCID: PMC4091555
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29670

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