The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity.

The Journal of Biological Chemistry
Sabine MaerzStephan Seiler

Abstract

Secretory proteins are subjected to a stringent endoplasmic reticulum-based quality control system that distinguishes aberrant from correctly folded proteins. The cytoplasmic peptide:N-glycanase cleaves oligosaccharides from misfolded glycoproteins and prepares them for degradation by the 26 S proteasome. In contrast to abundant in vitro data on its enzymatic function, the in vivo relevance of peptide:N-glycanase activity remains unclear. Here we show that the PNG1 ortholog from the filamentous ascomycete Neurospora crassa is an essential protein, and its deletion results in strong polarity defects. PNG1 and its predicted binding partner RAD23 have distinct functions in N. crassa and are involved in cell wall integrity and DNA repair, respectively. Moreover, wild type PNG1 has substitutions in essential catalytic amino acids, and its deglycosylation activity is lost. These substitutions are conserved in many PNG1 orthologs of the fungal kingdom, implying a so far unrecognized enzyme-independent function of PNG1 that may only become apparent in highly polar cells such as fungal hyphae.

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Citations

Jan 11, 2011·Journal of Biochemistry·Atsushi KatoTadashi Suzuki
Nov 10, 2013·PloS One·Yvonne HeiligStephan Seiler
Sep 15, 2017·ELife·Liping Zhang, Kelly G Ten Hagen
Jan 30, 2014·Médecine sciences : M/S·Isabelle ChantretStuart Moore
Feb 11, 2021·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Makoto AsahinaTadashi Suzuki
Jun 15, 2021·Molecular Brain·Makoto AsahinaTadashi Suzuki
Jun 7, 2011·Fungal Biology·Meritxell RiquelmeMichael K Watters
Nov 19, 2021·Journal of Biochemistry·Hiroto Hirayama, Tadashi Suzuki
Jun 5, 2012·Biochimica Et Biophysica Acta·Yuki Masahara-NegishiTadashi Suzuki
Jul 17, 2012·Fungal Genetics and Biology : FG & B·Georgios D TzelepisMagnus Karlsson

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