The ISWI remodeler in plants: protein complexes, biochemical functions, and developmental roles
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Imitation Switch (ISWI) is a member of the ATP-dependent chromatin remodeling factor family, whose members move or restructure nucleosomes using energy derived from ATP hydrolysis. ISWI proteins are conserved in eukaryotes and usually form complexes with DDT (DNA-binding homeobox and different transcription factors)-domain proteins. Here, we review recent research on ISWI in the model plant Arabidopsis thaliana (AtISWI). AtISWI forms complexes with AtDDT-domain proteins, many of which have domain structures that differ from those of DDT-domain proteins in yeast and animals. This might suggest that plant ISWI complexes have unique roles. In vivo studies have shown that AtISWI is involved in the formation of the evenly spaced pattern of nucleosome arrangement in gene bodies—this pattern is associated with high transcriptional levels of genes. In addition, AtISWI and the AtDDT-domain protein RINGLET (RLT) are involved in many developmental processes in A. thaliana, including meristem fate transition and organ formation. Studies on the functions of AtISWI may shed light on how chromatin remodeling functions in plants and also provide new information about the evolution of ISWI remodeling complexes in eukaryotes.
KeywordsArabidopsis thaliana ISWI RLT ATP-dependent chromatin remodeling Plant epigenetics DDT domain
The authors apologize for references not cited due to space limitations. This work was supported by grants from the National Natural Science Foundation of China (31630007/31422005/81471667), National Basic Research Program of China (973 Program, 2012CB910503), the Key Research Program of the Chinese Academy of Sciences (QYZDB-SSW-SMC010), and Youth Innovation Promotion Association CAS (2014241).
Compliance with ethical standards
This article does not contain any studies with human participants or animals performed by any of the authors.
Conflict of interest
The authors declare that they have no competing interests.
Glossary of domains and motifs in ISWI complexes
Interaction with methylated histones (Wysocka et al. 2006)
Interaction with acetylated histones (Dhalluin et al. 1999)
DNA binding (Fyodorov and Kadonaga 2002)
Putative binding activity with DNA cis elements (Mukherjee et al. 2009)
Involved in proteolytic cleavage of PTM in response to retrograde signals (Sun et al. 2011)
Unknown, possibly involved in chromatin regulation (Aravind and Iyer 2012)
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