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Correction for Strasser et al., Plant Physiol. 145 (1) 5-16.
Plant Physiology 147:931

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CORRECTIONS

CORRECTIONS

Vol. 145: 5–16, 2007

Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E., Glössl J., Altmann F., Steinkellner H., and Mach L. Enzymatic Properties and Subcellular Localization of Arabidopsis β-N-Acetylhexosaminidases.

The authors regret that the enzymatic properties of HEXO3 reported in this article are partially incorrect. This is due to the previously unnoticed inadvertent deletion of a single base pair close to the 3' end of the HEXO3 coding region that occurred during construction of the respective expression plasmid. The ensuing frame-shift changed the last five amino acids of HEXO3 and resulted in the elongation of the protein by 27 amino acids. In particular, the mutation removed a residue (Cys-532) required for proper function of this class of β-N-acetylhexosaminidases. Our original results indicated that the capacity of HEXO3 to degrade N-glycans and chitooligosaccharides is much lower than that of the closely related enzyme HEXO1. This suggested that HEXO1 is the β-N-acetylhexosaminidase largely responsible for N-glycan trimming in Arabidopsis. We have now expressed the authentic HEXO3 sequence in insect cells and have found that this enzyme is in fact similarly potent as HEXO1 in terms of degradation of N-glycan substrates and pyridylaminated chitotriose. In contrast to our original conclusions, these results demonstrate that HEXO1 and HEXO3 have comparable enzymatic properties and thus differ mainly in their subcellular localization.

A detailed description of the new data has been posted online as supplemental data.


   FOOTNOTES
 
www.plantphysiol.org/cgi/doi/10.1104/pp.104.900260





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