Topic
Multiprotein complex
About: Multiprotein complex is a research topic. Over the lifetime, 494 publications have been published within this topic receiving 33061 citations.
Papers published on a yearly basis
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Papers
TL;DR: Seven proteins function together in a complex required for exocytosis, and not other intracellular trafficking steps, the Exocyst, which is named after the yeast Saccharomyces cerevisiae.
Abstract: In the yeast Saccharomyces cerevisiae, the products of at least 15 genes are involved specifically in vesicular transport from the Golgi apparatus to the plasma membrane. Previously, we have shown that three of these genes, SEC6, SEC8 and SEC15, encode components of a multisubunit complex which localizes to the tip of the bud, the predominant site of exocytosis in S. cerevisiae. Mutations in three more of these genes, SEC3, SEC5 and SEC10, were found to disrupt the subunit integrity of the Sec6-Sec8-Sec15 complex, indicating that these genes may encode some of the remaining components of this complex. To examine this possibility, we cloned and sequenced the SEC5 and SEC10 genes, disrupted them, and either epitope tagged them (Sec5p) or prepared polyclonal antisera (Sec10p) to them for co-immunoprecipitation studies. Concurrently, we biochemically purified the remaining unidentified polypeptides of the Sec6-Sec8-Sec15 complex for peptide microsequencing. The genes encoding these components were identified by comparison of predicted amino acid sequences with those obtained from peptide microsequencing of the purified complex components. In addition to Sec6p, Sec8p and Sec15p, the complex contains the proteins encoded by SEC3, SEC5, SEC10 and a novel gene, EXO70. Since these seven proteins function together in a complex required for exocytosis, and not other intracellular trafficking steps, we have named it the Exocyst.
899 citations
TL;DR: Genetic interactions suggest a role for YfgL, one of the lipoprotein components of the protein assembly complex, in a homeostatic control mechanism that coordinates the overall OM assembly process.
778 citations
TL;DR: The Mediator is an evolutionarily conserved, multiprotein complex that is a key regulator of protein-coding genes in metazoan cells and can interact with and coordinate the action of numerous other co-activators and co-repressors, including those acting at the level of chromatin.
Abstract: The Mediator is an evolutionarily conserved, multiprotein complex that is a key regulator of protein-coding genes. In metazoan cells, multiple pathways that are responsible for homeostasis, cell growth and differentiation converge on the Mediator through transcriptional activators and repressors that target one or more of the almost 30 subunits of this complex. Besides interacting directly with RNA polymerase II, Mediator has multiple functions and can interact with and coordinate the action of numerous other co-activators and co-repressors, including those acting at the level of chromatin. These interactions ultimately allow the Mediator to deliver outputs that range from maximal activation of genes to modulation of basal transcription to long-term epigenetic silencing.
768 citations
TL;DR: The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein and found that the ordered assembly of these components on the nascent chain forms a high molecular mass complex.
Abstract: The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the chaperonin TRiC. The ordered assembly of these components on the nascent chain forms a high molecular mass complex that allows the cotranslational formation of protein domains and the completion of folding once the chain is released from the ribosome.
684 citations
TL;DR: A Xenopus oocyte model system shows that a variety of hyperedited, inosine-containing RNAs are specifically retained in the nucleus, and provides evidence that one function of the complex identified here is to anchor hyperedite RNAs to the nuclear matrix, while allowing selectively edited mRNAs to be exported.
515 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 2 |
| 2024 | 4 |
| 2023 | 5 |
| 2022 | 15 |
| 2021 | 11 |
| 2020 | 14 |