ArticleThe EMBO journal1999
A trans-acting peptide activates the yeast a1 repressor by raising its DNA-binding affinity.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Establishing an unusual cell type: how to make a dikaryon.Current opinion in microbiology · 2010Review
- Cognate Site Identifier analysis reveals novel binding properties of the Sex Inducer homeodomain proteins of Cryptococcus neoformans.Molecular microbiology · 2009Article
- Sex-specific homeodomain proteins Sxi1alpha and Sxi2a coordinately regulate sexual development in Cryptococcus neoformans.Eukaryotic cell · 2005Article
- Arm-domain interactions can provide high binding cooperativity.Protein science : a publication of the Protein Society · 2004Article
- Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.Protein science : a publication of the Protein Society · 2003Article
- The role of rigidity in DNA looping-unlooping by AraC.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Life history and developmental processes in the basidiomycete Coprinus cinereus.Microbiology and molecular biology reviews : MMBR · 2000Review
- Phosphorylation represses Ets-1 DNA binding by reinforcing autoinhibition.Genes & development · 2000Article
- Auto-inhibition of Ets-1 is counteracted by DNA binding cooperativity with core-binding factor alpha2.Molecular and cellular biology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The cooperative binding of gene regulatory proteins to DNA is a common feature of transcriptional control in both prokaryotes and eukaryotes. It is generally viewed as a simple energy coupling, through protein-protein interactions, of two or more DNA-binding proteins. In this paper, we show that the simple view does not account for the cooperative DNA binding of a1 and alpha2, two homeodomain proteins from budding yeast. Rather, we show through the use of chimeric proteins and synthetic peptides that, upon heterodimerization, alpha2 instructs a1 to bind DNA. This change is induced by contact with a peptide contributed by alpha2, and this contact converts a1 from a weak to a strong DNA-binding protein. This explains, in part, how high DNA-binding specificity is achieved only when the two gene regulatory proteins conjoin. We also provide evidence that features of the a1-alpha2 interaction can serve as a model for other examples of protein-protein interactions, including that between the herpes virus transcriptional activator VP16 and the mammalian homeodomain-containing protein Oct-l.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.