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Genes 2017, 8(9), 211; doi:10.3390/genes8090211

Two Archaeal RecJ Nucleases from Methanocaldococcus jannaschii Show Reverse Hydrolysis Polarity: Implication to Their Unique Function in Archaea

1
State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China
2
National Center for Protein Science, Chinese Academy of Sciences, Shanghai 201204, China
3
Department of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA
4
State Key Laboratory of Ocean Engineering, School of Naval Architecture, Ocean and Civil Engineering, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Eishi Noguchi
Received: 24 June 2017 / Revised: 16 August 2017 / Accepted: 17 August 2017 / Published: 24 August 2017
(This article belongs to the Special Issue DNA Replication Controls)
View Full-Text   |   Download PDF [3914 KB, uploaded 24 August 2017]   |  

Abstract

Bacterial nuclease RecJ, which exists in almost all bacterial species, specifically degrades single-stranded (ss) DNA in the 5′ to 3′ direction. Some archaeal phyla, except Crenarchaea, also encode RecJ homologs. Compared with bacterial RecJ, archaeal RecJ exhibits a largely different amino acid sequence and domain organization. Archaeal RecJs from Thermococcus kodakarensis and Pyrococcus furiosus show 5′→3′ exonuclease activity on ssDNA. Interestingly, more than one RecJ exists in some Euryarchaeota classes, such as Methanomicrobia, Methanococci, Methanomicrobia, Methanobacteria, and Archaeoglobi. Here we report the biochemical characterization of two RecJs from Methanocaldococcus jannaschii, the long RecJ1 (MJ0977) and short RecJ2 (MJ0831) to understand their enzymatic properties. RecJ1 is a 5′→3′ exonuclease with a preference to ssDNA; however, RecJ2 is a 3′→5′ exonuclease with a preference to ssRNA. The 5′ terminal phosphate promotes RecJ1 activity, but the 3′ terminal phosphate inhibits RecJ2 nuclease. Go-Ichi-Ni-San (GINS) complex does not interact with two RecJs and does not promote their nuclease activities. Finally, we discuss the diversity, function, and molecular evolution of RecJ in archaeal taxonomy. Our analyses provide insight into the function and evolution of conserved archaeal RecJ/eukaryotic Cdc45 protein. View Full-Text
Keywords: archaeal RecJ; Cdc45-MCM-GINS; nuclease; GINS; interaction archaeal RecJ; Cdc45-MCM-GINS; nuclease; GINS; interaction
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MDPI and ACS Style

Yi, G.-S.; Song, Y.; Wang, W.-W.; Chen, J.-N.; Deng, W.; Cao, W.; Wang, F.-P.; Xiao, X.; Liu, X.-P. Two Archaeal RecJ Nucleases from Methanocaldococcus jannaschii Show Reverse Hydrolysis Polarity: Implication to Their Unique Function in Archaea. Genes 2017, 8, 211.

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