Dataset Information

MEAF6 is essential for proliferation and plays a role in the assembly of KAT7 complexes

ABSTRACT: MEAF6 is essential for proliferation and plays a role in the assembly of KAT7 complexes.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Hitoshi Niwa

PROVIDER: PXD020422 | JPOST Repository | Wed Sep 23 00:00:00 BST 2020

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	1_Meaf6iKO_Myst2_IP_rep1.raw	Raw
	2_Meaf6iKO_Myst2_IP_rep2.raw	Raw
	3_Meaf6iKO_Myst2_IP_rep3.raw	Raw
	4_Meaf6iKO_Tx_Myst2_IP_rep1.raw	Raw
	5_Meaf6iKO_Tx_Myst2_IP_rep2.raw	Raw

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Publications

MEAF6 is essential for cell proliferation and plays a role in the assembly of KAT7 complexes.

Matsuura Kumi K Tani Naoki N Usuki Shingo S Torikai-Nishikawa Satomi S Okano Masaki M Niwa Hitoshi H

Experimental cell research 20200909 1

Myst family genes encode lysine acetyltransferases that mainly mediate histone acetylation to control transcription, DNA replication and DNA damage response. They form tetrameric complexes with PHD-finger proteins (Brpfs or Jades) and small non-catalytic subunits Ing4/5 and Meaf6. Although all the components of the complex are well-conserved from yeast to mammals, the function of Meaf6 and its homologs has not been elucidated in any species. Here we revealed the role of Meaf6 utilizing inducible ...[more]

PMID: 32918898

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Project description:Folding of newly synthesized proteins to the native state is a major challenge within the crowded cellular environment, since non-productive interactions can lead to misfolding, aggregation and degradation1. Cells cope with this challenge by coupling synthesis with polypeptide folding and by employing molecular chaperones to safeguard folding already cotranslationally2. However, little is known about the final step of folding, the assembly of polypeptides into complexes, although most of the cellular proteome forms oligomeric assemblies3. In prokaryotes, a proof-of-concept study showed that assembly of heterodimeric luciferase is an organized cotranslational process, facilitated by spatially confined translation of the subunits encoded on a polycistronic mRNA4. In eukaryotes, however, fundamental differences such as rarity of polycistronic mRNAs and different chaperone constellations raise the question whether assembly is also coordinated with translation. Here we provide a systematic and mechanistic analysis of protein complex assembly in eukaryotes using ribosome profiling. We determined the in vivo nascent subunits interactions of 12 hetero-oligomeric protein complexes of Saccharomyces cerevisiae at near-residue resolution. We find 9 complexes assemble cotranslationally; the 3 complexes that do not show cotranslational interactions are regulated by dedicated assembly chaperones5-7. Cotranslational assembly often occurs uni-directionally, with one fully synthesized subunit engaging its nascent partner subunit(s), thereby counteracting its aggregation propensity. The onset of cotranslational subunit association coincides sharply with full exposure of the nascent interaction domain at the ribosomal tunnel exit. The action of the ribosome-associated Hsp70 chaperone Ssb8 is coordinated with assembly. Ssb transiently engages partially synthesized interaction domains, then dissociates before the onset of partner subunit association, presumably to prevent premature assembly interactions. Our study shows that cotranslational subunit association is a prevalent mechanism for hetero-oligomers assembly in yeast and indicates that translation, folding and assembly of protein complexes are integrated processes in eukaryotes.