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The DUF328 family member YaaA is a DNA-binding protein with a novel fold

Janani Prahlad, Yifeng Yuan, Jiusheng Lin, Chou-Wei Chang, Dirk Iwata‐Reuyl, Yilun Liu, Valérie de Crécy‐Lagard, Mark A. Wilson

2020Journal of Biological Chemistry11 citationsDOIOpen Access PDF

Abstract

with dissociation equilibrium constants of 200-300 nm YaaA binds DNA with positive cooperativity, forming multiple shifted species in electrophoretic mobility shift assays. The 1.65-Å resolution X-ray crystal structure of YaaA reveals that the protein possesses a new fold that we name the cantaloupe fold. YaaA has a positively charged cleft and a helix-hairpin-helix DNA-binding motif found in other DNA repair enzymes. Our results demonstrate that YaaA is a new type of DNA-binding protein associated with the oxidative stress response and that this molecular function is likely conserved in other DUF328 family members.

Topics & Concepts

Replication protein ADNA repairDNABiologyHolliday junctionProtein–DNA interactionCooperativityHMG-boxProtein familyDNA-binding proteinDNA damageGeneRecombinant DNAGeneticsBiochemistryMolecular biologyTranscription factorDNA Repair MechanismsBacterial Genetics and BiotechnologyPhotosynthetic Processes and Mechanisms
The DUF328 family member YaaA is a DNA-binding protein with a novel fold | Litcius