Saccharomyces cerevisiae linker histone Hho1p is not essential for cell 
viability, and very little is known about its function in vivo. We show that 
deletion of HHO1 (hho1Delta) suppresses the defect in transcriptional silencing 
caused by a mutation in the globular domain of histone H4. hho1Delta also 
suppresses the reduction in HML silencing by the deletion of SIR1 that is 
involved in the establishment of silent chromatin at HML. We further show that 
hho1Delta suppresses changes in silent chromatin structure caused by the histone 
H4 mutation and sir1Delta. These results suggest that HHO1 plays a negative role 
in transcriptionally silent chromatin. We also provide evidence that Hho1p 
hinders the de novo establishment of silent chromatin but does not affect the 
stability of preexistent silent chromatin. Unlike canonical linker histones in 
higher eukaryotes that have a single conserved globular domain, Hho1p possesses 
two globular domains. We show that the carboxyl-terminal globular domain of 
Hho1p is dispensable for its function, suggesting that the mode of Hho1p action 
is similar to that of canonical linker histones.