Premium
Characterization of Yeast High Mobility Group Protein HMO2
Author(s) -
Ray Sreerupa,
Grove Anne
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a283-b
Subject(s) - high mobility group , dna supercoil , chromatin , biology , dna , hmg box , non histone protein , saccharomyces cerevisiae , microbiology and biotechnology , histone , gene , topoisomerase , dna binding protein , genetics , dna replication , transcription factor
High Mobility Group (HMGB) proteins are non‐histone chromosomal proteins which are common in eukaryotes. They bind to DNA in a non‐sequence specific manner and participate in chromatin functions and gene regulation. HMO2 from Saccharomyces cerevisiae is a HMGB protein with two HMG like domains‐ Box‐A and Box‐B. HMO2 is a component of the DNA damage‐dependent chromatin‐remodelling complex, INO8O. The gene encoding HMO2 was cloned from yeast genomic DNA. HMO2 was expressed in E.coli Rosetta Blue and the protein was purified using nickel affinity chromatography. DNA binding assays indicate that HMO2 binds to supercoiled DNA (pGEM5) with higher affinity than linear DNA. Also, HMO2 constrains DNA supercoils in the presence of topoisomerase I. This is in contrast to the homolog HMO1 which fails to supercoil DNA. Consistent with distinct functions of these closely related proteins, HMO2 does not rescue an hmo1 knockout phenotype.