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DOI | 10.1007/s11103-016-0519-y |
Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana | |
Roy, Adrita1; Dutta, Arkajyoti4; Roy, Dipan1; Ganguly, Payel1; Ghosh, Ritesh2; Kar, Rajiv K.3; Bhunia, Anirban3; Mukhobadhyay, Jayanta4; Chaudhuri, Shubho1 | |
通讯作者 | Chaudhuri, Shubho |
来源期刊 | PLANT MOLECULAR BIOLOGY
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ISSN | 0167-4412 |
EISSN | 1573-5028 |
出版年 | 2016 |
卷号 | 92期号:3页码:371-388 |
英文摘要 | ARID-HMG DNA-binding proteins represent a novel group of HMG-box containing protein family where the AT-rich interaction domain (ARID) is fused with the HMG-box domain in a single polypeptide chain. ARID-HMG proteins are highly plant specific with homologs found both in flowering plants as well as in moss such as Physcomitrella. The expression of these proteins is ubiquitous in plant tissues and primarily localises in the cell nucleus. HMGB proteins are involved in several nuclear processes, but the role of ARID-HMG proteins in plants remains poorly explored. Here, we performed DNA-protein interaction studies with Arabidopsis ARID-HMG protein HMGB11 (At1g55650) to understand the functionality of this protein and its individual domains. DNA binding assays revealed that AtHMGB11 can bind double-stranded DNA with a weaker affinity (K-d = 475 +/- 17.9 nM) compared to Arabidopsis HMGB1 protein (K-d = 39.8 +/- 2.68 nM). AtHMGB11 also prefers AT-rich DNA as a substrate and shows structural bias for supercoiled DNA. Molecular docking of the DNA-AtHMGB11 complex indicated that the protein interacts with the DNA major groove, mainly through its ARID domain and the junction region connecting the ARID and the HMG-box domain. Also, predicted by the docking model, mutation of Lys(85) from the ARID domain and Arg(199) & Lys(202) from the junction region affects the DNA binding affinity of AtHMGB11. In addition, AtHMGB11 and its truncated form containing the HMG-box domain can not only promote DNA mini-circle formation but are also capable of inducing negative supercoils into relaxed plasmid DNA suggesting the involvement of this protein in several nuclear events. Overall, the study signifies that both the ARID and the HMG-box domain contribute to the optimal functioning of ARID-HMG protein in vivo. |
英文关键词 | HMG-box protein ARID-HMG Arabidopsis thaliana DNA binding DNA bending DNA supercoiling |
类型 | Article |
语种 | 英语 |
国家 | India ; South Korea |
收录类别 | SCI-E |
WOS记录号 | WOS:000385047500009 |
WOS关键词 | DNA-BINDING PROTEINS ; HISTONE H1 ; ARCHITECTURAL ELEMENTS ; LINKER HISTONES ; CHROMATIN FIBER ; MAIZE HMGA ; MOBILITY ; NUCLEOSOME ; TRANSCRIPTION ; FAMILY |
WOS类目 | Biochemistry & Molecular Biology ; Plant Sciences |
WOS研究方向 | Biochemistry & Molecular Biology ; Plant Sciences |
资源类型 | 期刊论文 |
条目标识符 | http://119.78.100.177/qdio/handle/2XILL650/195543 |
作者单位 | 1.Bose Inst, Div Plant Biol, Kolkata 700054, India; 2.Yeungnam Univ, Sch Biotechnol, Gyongsan 712749, South Korea; 3.Bose Inst, Dept Biophys, Kolkata 700054, India; 4.Bose Inst, Dept Chem, Kolkata 700054, India |
推荐引用方式 GB/T 7714 | Roy, Adrita,Dutta, Arkajyoti,Roy, Dipan,et al. Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana[J],2016,92(3):371-388. |
APA | Roy, Adrita.,Dutta, Arkajyoti.,Roy, Dipan.,Ganguly, Payel.,Ghosh, Ritesh.,...&Chaudhuri, Shubho.(2016).Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana.PLANT MOLECULAR BIOLOGY,92(3),371-388. |
MLA | Roy, Adrita,et al."Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana".PLANT MOLECULAR BIOLOGY 92.3(2016):371-388. |
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