Cpf1 protein induced bending of yeast centromere DNA element I

The centromere complex is a multicomponent structure essential for faithful chromosome transmission. Here we show that the S. cerevisiae centromere protein Cpf1 bends centromere DNA element I (CDEI) with the bend angle ranging from 66 degrees to 71 degrees. CDEI DNA sequences that carry point mutati...

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Bibliographic Details
Published in:Nucleic acids research 1993-10, Vol.21 (20), p.4726-4733
Main Authors: Niedenthal, R.K, Sen-Gupta, M, Wilmen, A, Hegemann, J.H
Format: Article
Language:English
Subjects:
Base Sequence
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Biological and medical sciences
Centromere - chemistry
centromeres
Chromatin. Chromosome
DNA
dna bending
DNA, Fungal - chemistry
DNA-binding proteins
DNA-Binding Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
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Summary:The centromere complex is a multicomponent structure essential for faithful chromosome transmission. Here we show that the S. cerevisiae centromere protein Cpf1 bends centromere DNA element I (CDEI) with the bend angle ranging from 66 degrees to 71 degrees. CDEI DNA sequences that carry point mutations which lead to reduced Cpf1 binding affinity and in vivo centromere activity are still able to show bending. The Cpf1 induced bend is directed towards the major groove with the bend center located in CDEI. An intrinsic bend cannot replace the Cpf1 induced DNA bend for in vivo centromere function. An in vivo phasing experiment suggests that both the distance and the correct spatial arrangement of the CDEI/Cpf1 complex to CDEII and CDEIII are important for optimal centromere function.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/21.20.4726