Characterization of a periplasmic S1-like nuclease coded by the Mesorhizobium loti symbiosis island

Biochemical and Biophysical Research Communications
Maxim PimkinAnthony T Yeung

Abstract

DNA sequences encoding hypothetical proteins homologous to S1 nuclease from Aspergillus oryzae are found in many organisms including fungi, plants, pathogenic bacteria, and eukaryotic parasites. One of these is the M1 nuclease of Mesorhizobium loti which we demonstrate herein to be an enzymatically active, soluble, and stable S1 homolog that lacks the extensive mannosyl-glycosylation found in eukaryotic S1 nuclease homologs. We have expressed the cloned M1 protein in M. loti and purified recombinant native M1 to near homogeneity and have also isolated a homogeneous M1 carboxy-terminal hexahistidine tag fusion protein. Mass spectrometry and N-terminal Edman degradation sequencing confirmed the protein identity. The enzymatic properties of the purified M1 nuclease are similar to those of S1. At acidic pH M1 is 25 times more active on single-stranded DNA than on double-stranded DNA and 3 times more active on single-stranded DNA than on single-stranded RNA. At neutral pH the RNase activity of M1 exceeds the DNase activity. M1 nicks supercoiled RF-I plasmid DNA and rapidly cuts the phosphodiester bond across from the nick in the resultant relaxed RF-II plasmid DNA. Therefore, M1 represents an active bacterial S1 homolog in spite of ...Continue Reading

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Citations

Jun 8, 2011·Marine Biotechnology·Larissa A BalabanovaValery A Rasskazov
Jun 28, 2011·Applied and Environmental Microbiology·R G AmachawadiT G Nagaraja
Jun 5, 2007·BMC Biotechnology·Maxim PimkinAnthony T Yeung
Jun 3, 2014·BMC Genomics·Aminael Sánchez-RodríguezKathleen Marchal
Nov 29, 2017·Molecular Plant-microbe Interactions : MPMI·Zhiwei HuangMinliang Guo

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