Phylogenetic Analysis and In Vitro Bifunctional Nuclease Assay of Arabidopsis BBD1 and BBD2
| Autor: | Jeong Sheop Shin, Min Kyoung You, Won Mi So, A K M Mahmudul Huque |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
Arabidopsis Pharmaceutical Science 01 natural sciences Homology (biology) DUF151 Analytical Chemistry law.invention law Drug Discovery Magnesium nuclease Phylogeny 0303 health sciences Deoxyribonucleases biology Chemistry OmBBD Eukaryota Recombinant Proteins Biochemistry Chemistry (miscellaneous) Recombinant DNA Molecular Medicine Domain of unknown function AtBBD1 Cofactor Article lcsh:QD241-441 Evolution Molecular 03 medical and health sciences lcsh:Organic chemistry Protein Domains Viridiplantae Amino Acid Sequence Physical and Theoretical Chemistry 030304 developmental biology Nuclease Manganese Bacteria Sequence Homology Amino Acid Arabidopsis Proteins Organic Chemistry Oryza biology.organism_classification Endonucleases Archaea Yeast biology.protein Protein Multimerization Sequence Alignment Chlamydomonas reinhardtii 010606 plant biology & botany |
| Zdroj: | Molecules Volume 25 Issue 9 Molecules, Vol 25, Iss 2169, p 2169 (2020) |
| ISSN: | 1420-3049 |
| Popis: | Nucleases are a very diverse group of enzymes that play important roles in many crucial physiological processes in plants. We previously reported that the highly conserved region (HCR), domain of unknown function 151 (DUF151) and UV responsive (UVR) domain-containing OmBBD is a novel nuclease that does not share homology with other well-studied plant nucleases. Here, we report that DUF151 domain-containing proteins are present in bacteria, archaea and only Viridiplantae kingdom of eukarya, but not in any other eukaryotes. Two Arabidopsis homologs of OmBBD, AtBBD1 and AtBBD2, shared 43.69% and 44.38% sequence identity and contained all three distinct domains of OmBBD. We confirmed that the recombinant MBP-AtBBD1 and MBP-AtBBD2 exhibited non-substrate-specific DNase and RNase activity, like OmBBD. We also found that a metal cofactor is not necessarily required for DNase activity of AtBBD1 and AtBBD2, but their activities were much enhanced in the presence of Mg2+ or Mn2+. Using a yeast two-hybrid assay, we found that AtBBD1 and AtBBD2 each form a homodimer but not a heterodimer and that the HCR domain is possibly crucial for dimerization. |
| Databáze: | OpenAIRE |
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