Structural basis of DNA replication origin recognition by human Orc6 protein binding with DNA | Zendy

Naining Xu | Zendy; Yingying You | Zendy; Changdong Liu | Zendy; Maxim Balasov | Zendy; Lee Tung Lun | Zendy; Yanyan Geng | Zendy; Chun Po Fung | Zendy; Haitao Miao | Zendy; Honglei Tian | Zendy; To To Choy | Zendy; Shi Xiao | Zendy; Zhuming Fan | Zendy; Bo Zhou | Zendy; Katarina Akhmetova | Zendy; Rahman Ud Din | Zendy; Hongyu Yang | Zendy; Quan Hao | Zendy; PeiYuan Qian | Zendy; Igor Chesnokov | Zendy; Guang Zhu | Zendy

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Structural basis of DNA replication origin recognition by human Orc6 protein binding with DNA

Author(s) -

Naining Xu,

Yingying You,

Changdong Liu,

Maxim Balasov,

Lee Tung Lun,

Yanyan Geng,

Chun Po Fung,

Haitao Miao,

Honglei Tian,

To To Choy,

Shi Xiao,

Zhuming Fan,

Bo Zhou,

Katarina Akhmetova,

Rahman Ud Din,

Hongyu Yang,

Quan Hao,

PeiYuan Qian,

Igor Chesnokov,

Guang Zhu

Publication year - 2020

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkaa751

Subject(s) - biology , origin recognition complex , dna replication , hmg box , dna , replication protein a , protein subunit , replication factor c , eukaryotic dna replication , control of chromosome duplication , dna clamp , dna binding domain , seqa protein domain , pre replication complex , genetics , origin of replication , ter protein , microbiology and biotechnology , dna binding protein , transcription factor , gene , reverse transcriptase , rna

The six-subunit origin recognition complex (ORC), a DNA replication initiator, defines the localization of the origins of replication in eukaryotes. The Orc6 subunit is the smallest and the least conserved among ORC subunits. It is required for DNA replication and essential for viability in all species. Orc6 in metazoans carries a structural homology with transcription factor TFIIB and can bind DNA on its own. Here, we report a solution structure of the full-length human Orc6 (HsOrc6) alone and in a complex with DNA. We further showed that human Orc6 is composed of three independent domains: N-terminal, middle and C-terminal (HsOrc6-N, HsOrc6-M and HsOrc6-C). We also identified a distinct DNA-binding domain of human Orc6, named as HsOrc6-DBD. The detailed analysis of the structure revealed novel amino acid clusters important for the interaction with DNA. Alterations of these amino acids abolish DNA-binding ability of Orc6 and result in reduced levels of DNA replication. We propose that Orc6 is a DNA-binding subunit of human/metazoan ORC and may play roles in targeting, positioning and assembling the functional ORC at the origins.

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