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The transcription factor YY 2 has less momentous properties of an intrinsically disordered protein than its paralog YY 1
Author(s) -
Figiel Małgorzata,
Łakomska Julia,
Miłek Piotr,
DziedzickaWasylewska Marta,
Górecki Andrzej
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13457
Subject(s) - peptide yy , transcription factor , biology , microbiology and biotechnology , genetics , gene , receptor , neuropeptide y receptor , neuropeptide
The transcription factor YY 2 is a recently discovered paralog of YY 1. The two proteins exhibit substantial sequence similarity and partially similar transcriptional activity. They recognize the same DNA sequence in vitro yet bind different promoters in vivo . YY 1 comprises two structurally distinct parts: an intrinsically disordered regulatory part and a compact DNA ‐binding domain. The structure of YY 2 is yet unknown. We show that YY 2 is structurally similar to YY 1, although the conformational state of YY 2 is more ordered, as shown by its composition, hydrodynamic properties, spectroscopic signal, and proteolytic susceptibility. As such, YY 2's range of molecular partners might be distinct from that of YY 1. This could explain different effects of YY 1 and YY 2 on gene expression patterns and the mechanism of YY proteins in transcriptional regulation.