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The structure of the FYR domain of transforming growth factor beta regulator 1
Author(s) -
GarcíaAlai María M.,
Allen Mark D.,
Joerger Andreas C.,
Bycroft Mark
Publication year - 2010
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.404
Subject(s) - regulator , chromatin , biology , interactor , sequence motif , microbiology and biotechnology , genetics , dna , gene
Many chromatin‐associated proteins contain two sequence motifs rich in phenylalanine/tyrosine residues of unknown function. These so‐called FYRN and FYRC motifs are also found in transforming growth factor beta regulator 1 (TBRG1)/nuclear interactor of ARF and MDM2 (NIAM), a growth inhibitory protein that also plays a role in maintaining chromosomal stability. We have solved the structure of a fragment of TBRG1, which encompasses both of these motifs. The FYRN and FYRC regions each form part of a single folded module (the FYR domain), which adopts a novel α + β fold. Proteins such as the histone H3K4 methyltransferases trithorax and mixed lineage leukemia (MLL), in which the FYRN and FYRC regions are separated by hundreds of amino acids, are expected to contain FYR domains with a large insertion between two of the strands of the β‐sheet.