Evolutionarily conserved E(y)2/Sus1 protein is essential for the barrier activity of Su(Hw)-dependent insulators in Drosophila.
Chromatin insulators affect interactions between promoters and enhancers/silencers and function as barriers for spreading of repressive chromatin. The Su(Hw) protein is responsible for activity of the best-studied Drosophila insulators. Here we demonstrate that an evolutionarily conserved protein, E(y)2/Sus1, is recruited to the Su(Hw) insulators via binding to the zinc-finger domain of Su(Hw). Partial inactivation of E(y)2 in a weak mutation, e(y)2(u1), impairs only the barrier, but not the enhancer-blocking, activity of the Su(Hw) insulators. Whereas neither su(Hw)(-) nor e(y)2(u1) affects fly viability, their combination proves lethal, testifying to functional interaction between Su(Hw) and E(y)2 in vivo. Apparently, different domains of Su(Hw) recruit proteins responsible for enhancer-blocking and for the barrier activity.
Kurshakova
Maria
M
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Maksimenko
Oksana
O
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Golovnin
Anton
A
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia; University of Oslo, Centre for Medical Studies in Russia, Moscow 119334, Russia.
Pulina
Maria
M
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Georgieva
Sofia
S
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia; University of Oslo, Centre for Medical Studies in Russia, Moscow 119334, Russia; Engelhardt Institute of Molecular Biology, Moscow 119334, Russia.
Georgiev
Pavel
P
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia. Electronic address: georgiev_p@mail.ru.
Krasnov
Aleksey
A
Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia; University of Oslo, Centre for Medical Studies in Russia, Moscow 119334, Russia. Electronic address: krasnov@go.ru.
D000818:Animals; D030801:Animals, Genetically Modified; D001665:Binding Sites; D017124:Conserved Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D004330:Drosophila / Q000235:genetics* / Q000378:metabolism*; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D019143:Evolution, Molecular; D017344:Genes, Insect; D009154:Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D020798:Two-Hybrid System Techniques; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D011994:Recombinant Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; C423782:e(y)2 protein, Drosophila; C083738:su(Hw) protein, Drosophila