File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The centromere and promoter factor 1 of yeast contains a dimerisation domain located carboxy-terminal to the bHLH domain

TitleThe centromere and promoter factor 1 of yeast contains a dimerisation domain located carboxy-terminal to the bHLH domain
Authors
Issue Date1992
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 1992, v. 20 n. 16, p. 4229-4236 How to Cite?
AbstractCPF1 is a basic helix - loop - helix (bHLH) protein required for optimal centromere function and for maintaining methionine independent growth in yeast. In this work, we show that the region carboxy-terminal to the bHLH domain of CPF1 is essential for CPF1 function in the cell and for dimerisation of CPF1 in solution. The C-terminus of CPF1 contains a potential long amphipathic helix with a hydrophobic face which could provide a suitable protein:protein interface. Point mutations in residues forming this hydrophobic face are sufficient to weaken the interaction between the protein and DNA. By fusing the DNA binding domain or the transcriptional activation domain of GAL4 to the C-terminal 87 amino acids of CPF1, we show that this region is sufficient for mediating protein:protein interactions in vivo. The C-terminal domain of CPF1 can be replaced by the leucine repeat region of the bHLHZIP protein USF and the hybrid CPF1-USF protein functions in vivo to provide normal centromere function and methionine independent growth. However, the CPF1-USF hybrid protein is unable to interact with CPF1 suggesting that a dimer of CPF1 is sufficient for maintaining methionine independent growth and normal centromere function.
Persistent Identifierhttp://hdl.handle.net/10722/178531
ISSN
2015 Impact Factor: 9.202
2015 SCImago Journal Rankings: 7.458
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorDowell, SJen_US
dc.contributor.authorTsang, JSHen_US
dc.contributor.authorMellor, Jen_US
dc.date.accessioned2012-12-19T09:48:15Z-
dc.date.available2012-12-19T09:48:15Z-
dc.date.issued1992en_US
dc.identifier.citationNucleic Acids Research, 1992, v. 20 n. 16, p. 4229-4236en_US
dc.identifier.issn0305-1048en_US
dc.identifier.urihttp://hdl.handle.net/10722/178531-
dc.description.abstractCPF1 is a basic helix - loop - helix (bHLH) protein required for optimal centromere function and for maintaining methionine independent growth in yeast. In this work, we show that the region carboxy-terminal to the bHLH domain of CPF1 is essential for CPF1 function in the cell and for dimerisation of CPF1 in solution. The C-terminus of CPF1 contains a potential long amphipathic helix with a hydrophobic face which could provide a suitable protein:protein interface. Point mutations in residues forming this hydrophobic face are sufficient to weaken the interaction between the protein and DNA. By fusing the DNA binding domain or the transcriptional activation domain of GAL4 to the C-terminal 87 amino acids of CPF1, we show that this region is sufficient for mediating protein:protein interactions in vivo. The C-terminal domain of CPF1 can be replaced by the leucine repeat region of the bHLHZIP protein USF and the hybrid CPF1-USF protein functions in vivo to provide normal centromere function and methionine independent growth. However, the CPF1-USF hybrid protein is unable to interact with CPF1 suggesting that a dimer of CPF1 is sufficient for maintaining methionine independent growth and normal centromere function.en_US
dc.languageengen_US
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/en_US
dc.relation.ispartofNucleic Acids Researchen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBasic Helix-Loop-Helix Leucine Zipper Transcription Factorsen_US
dc.subject.meshDna-Binding Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshFungal Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshLeucine Zippers - Geneticsen_US
dc.subject.meshMacromolecular Substancesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPlasmids - Geneticsen_US
dc.subject.meshSaccharomyces Cerevisiae - Geneticsen_US
dc.subject.meshSaccharomyces Cerevisiae Proteinsen_US
dc.titleThe centromere and promoter factor 1 of yeast contains a dimerisation domain located carboxy-terminal to the bHLH domainen_US
dc.typeArticleen_US
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_US
dc.identifier.authorityTsang, JSH=rp00792en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1093/nar/20.16.4229-
dc.identifier.pmid1508716-
dc.identifier.scopuseid_2-s2.0-0026656414en_US
dc.identifier.volume20en_US
dc.identifier.issue16en_US
dc.identifier.spage4229en_US
dc.identifier.epage4236en_US
dc.identifier.isiWOS:A1992JL46400016-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridDowell, SJ=7004419885en_US
dc.identifier.scopusauthoridTsang, JSH=7102483508en_US
dc.identifier.scopusauthoridMellor, J=7103106833en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats