ArticleProceedings of the National Academy of Sciences of the United States of America2000
A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- DNA binding by the MATα2 transcription factor controls its access to alternative ubiquitin-modification pathways.Molecular biology of the cell · 2018Article
- STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sites.Molecular biology of the cell · 2015Article
- The glucose signaling network in yeast.Biochimica et biophysica acta · 2013Review
- Mth1 regulates the interaction between the Rgt1 repressor and the Ssn6-Tup1 corepressor complex by modulating PKA-dependent phosphorylation of Rgt1.Molecular biology of the cell · 2013Article
- Pleiotropic corepressors Sin3 and Ssn6 interact with repressor Opi1 and negatively regulate transcription of genes required for phospholipid biosynthesis in the yeast Saccharomyces cerevisiae.Molecular genetics and genomics : MGG · 2011Article
- Corepressor-directed preacetylation of histone H3 in promoter chromatin primes rapid transcriptional switching of cell-type-specific genes in yeast.Molecular and cellular biology · 2010Article
- The short-lived Matalpha2 transcriptional repressor is protected from degradation in vivo by interactions with its corepressors Tup1 and Ssn6.Molecular and cellular biology · 2006Article
- Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals.The Biochemical journal · 2001Article
- Article
- Degradation elements coincide with cofactor binding sites in a short-lived transcription factor.Cellular logisticsReview
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tetratricopeptide repeat (TPR) is a 34-aa sequence motif, typically found in tandem clusters, that occurs in proteins of bacteria, archea, and eukaryotes. TPRs interact with other proteins, although few details on TPR-protein interactions are known. In this paper we show that a portion of a loop in the homeodomain of the DNA-binding protein alpha2 is required for its recognition by the TPRs of the corepressor Ssn6. The amino acid sequence of this loop is similar to the sequences recognized by the TPRs of an entirely different protein, Pex5, which directs peroxisomal import. We further show that alpha2 can be made to bind specifically in vitro to the TPRs of Pex5 and that a point mutation that disrupts the alpha2-Ssn6 interaction also disrupts the alpha2-Pex5 interaction. These results demonstrate that two different TPR proteins recognize their target by a similar mechanism, raising the possibility that other TPR-target interactions could occur through the same means.
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