NDLI: A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η

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Molecular BioSystems Vol - 7 Issue - 5

Molecular BioSystems Vol - 7 Issue - 4

Molecular BioSystems Vol - 7 Issue - 3

Molecular BioSystems Vol - 7 Issue - 2

Molecular BioSystems Vol -6

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Molecular BioSystems Vol -2

A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η

Content Provider	Royal Society of Chemistry (RSC)
Author	Johnson, Robert E. Haracska, Lajos Wang, Jialiang Prakash, Louise Ai, Yongxing Zhuang, Zhihao
Copyright Year	2011
Abstract	The ubiquitin binding zinc finger (UBZ) domain in the C-terminal portion of Polη has been found to interact with ubiquitin. However, the affinity between the Polη UBZ and ubiquitin was shown to be low with a previously reported Kd of 73–81 μM. This low-affinity binding between Polη UBZ and ubiquitin has been difficult to reconcile with its presumed role in translesion synthesis as suggested by genetic and cell biology studies. In this work, we constructed a minimal S. cerevisiae Polη UBZ domain and probed the Polη UBZ-ubiquitin interaction using a surface plasmon resonance (SPR) technique. Our quantitative binding data between the wild-type or mutant Polη UBZ and ubiquitin revealed an interesting divergence between the Polη UBZ from S. cerevisiae and humans. Moreover, we found that the C-terminal portion of yeast Polη (amino acid 515–632) binds ubiquitin with a much higher affinity than the minimal UBZ domain. Further, distinct ubiquitin-binding kinetics were observed for the C-terminal portion of Polη and the isolated UBZ domain. This observation raised the interesting possibility that the Polη C-terminal portion binds ubiquitin in a novel mode that affords higher affinity. Our findings have broader implication in understanding the generally weak interaction between the known ubiquitin-binding domains and ubiquitin.
Starting Page	1874
Ending Page	1882
Page Count	9
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	6
Journal	Molecular BioSystems
DOI	10.1039/c0mb00355g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Ubiquitin Weak interaction Dissociation constant UBZ Surface plasmon DNA repair C-terminus Zinc finger Gene regulatory network Surface plasmon resonance Mutation Molecular biology Saccharomyces cerevisiae
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Structure of the ubiquitin-binding zinc finger domain of human dna y-polymerase η. Embo reports 2007;8:247–251. [pubmed: 17304240.

A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η

The ubiquitin-binding domain of DNA polymerase η directly binds to DNA clamp PCNA and regulates translesion DNA synthesis.

Running title: role of polη ubz domain in tls (2007).

Mutations in the Ubiquitin Binding UBZ Motif of DNA Polymerase η Do Not Impair Its Function in Translesion Synthesis during Replication▿

Mutations in the ubiquitin binding ubz motif of dna polymerase (2007).

Gene of saccharomyces cerevisiae encoding a protein with a putative zinc finger dna-binding domain (1991).

The unusual UBZ domain of Saccharomyces cerevisiae polymerase η

Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase η

A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η

Similar Documents

Structure of the ubiquitin-binding zinc finger domain of human dna y-polymerase η. Embo reports 2007;8:247–251. [pubmed: 17304240.

A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η

The ubiquitin-binding domain of DNA polymerase η directly binds to DNA clamp PCNA and regulates translesion DNA synthesis.

Running title: role of polη ubz domain in tls (2007).

Mutations in the Ubiquitin Binding UBZ Motif of DNA Polymerase η Do Not Impair Its Function in Translesion Synthesis during Replication▿

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A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η