TY - JOUR
T1 - Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly
AU - Bertolini, Matilde
AU - Fenzl, Kai
AU - Kats, Ilia
AU - Wruck, Florian
AU - Tippmann, Frank
AU - Schmitt, Jaro
AU - Auburger, Josef Johannes
AU - Tans, Sander
AU - Bukau, Bernd
AU - Kramer, Günter
N1 - Accepted Author Manuscript
PY - 2021
Y1 - 2021
N2 - Accurate assembly of newly synthesized proteins into functional oligomers is crucial for cell activity. In this study, we investigated whether direct interaction of two nascent proteins, emerging from nearby ribosomes (co-co assembly), constitutes a general mechanism for oligomer formation. We used proteome-wide screening to detect nascent chain-connected ribosome pairs and identified hundreds of homomer subunits that co-co assemble in human cells. Interactions are mediated by five major domain classes, among which N-terminal coiled coils are the most prevalent. We were able to reconstitute co-co assembly of nuclear lamin in Escherichia coli, demonstrating that dimer formation is independent of dedicated assembly machineries. Co-co assembly may thus represent an efficient way to limit protein aggregation risks posed by diffusion-driven assembly routes and ensure isoform-specific homomer formation.
AB - Accurate assembly of newly synthesized proteins into functional oligomers is crucial for cell activity. In this study, we investigated whether direct interaction of two nascent proteins, emerging from nearby ribosomes (co-co assembly), constitutes a general mechanism for oligomer formation. We used proteome-wide screening to detect nascent chain-connected ribosome pairs and identified hundreds of homomer subunits that co-co assemble in human cells. Interactions are mediated by five major domain classes, among which N-terminal coiled coils are the most prevalent. We were able to reconstitute co-co assembly of nuclear lamin in Escherichia coli, demonstrating that dimer formation is independent of dedicated assembly machineries. Co-co assembly may thus represent an efficient way to limit protein aggregation risks posed by diffusion-driven assembly routes and ensure isoform-specific homomer formation.
UR - http://www.scopus.com/inward/record.url?scp=85099138187&partnerID=8YFLogxK
U2 - 10.1126/science.abc7151
DO - 10.1126/science.abc7151
M3 - Article
C2 - 33384371
AN - SCOPUS:85099138187
VL - 371
SP - 57
EP - 64
JO - Science
JF - Science
SN - 0036-8075
IS - 6524
M1 - eabc7151
ER -