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UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes
Plant cell wall synthesis requires a number of different nucleotide sugars which provide the building blocks of the different polymers. These nucleotide sugars are mainly provided by de novo synthesis but recycling pathways also contribute to the pools. The last enzyme of the recycling pathway is UD...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4002622/ https://www.ncbi.nlm.nih.gov/pubmed/23857351 http://dx.doi.org/10.4161/psb.25478 |
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author | Geserick, Claudia Tenhaken, Raimund |
author_facet | Geserick, Claudia Tenhaken, Raimund |
author_sort | Geserick, Claudia |
collection | PubMed |
description | Plant cell wall synthesis requires a number of different nucleotide sugars which provide the building blocks of the different polymers. These nucleotide sugars are mainly provided by de novo synthesis but recycling pathways also contribute to the pools. The last enzyme of the recycling pathway is UDP-sugar pyrophosphorylase (USP), a single copy gene in Arabidopsis, of which a knockout is lethal for pollen development. Here we analyze the dependency between USP enzyme activity and the upstream glucuronokinase. Gene silencing of USP by miRNA cause a concomitant reduction of USP and of glucuronokinase activity presumably to prevent the accumulation of sugar-1-phosphates interfering with normal metabolism and depleting the phosphate pool of the cell. |
format | Online Article Text |
id | pubmed-4002622 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-40026222014-04-30 UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes Geserick, Claudia Tenhaken, Raimund Plant Signal Behav Short Communication Plant cell wall synthesis requires a number of different nucleotide sugars which provide the building blocks of the different polymers. These nucleotide sugars are mainly provided by de novo synthesis but recycling pathways also contribute to the pools. The last enzyme of the recycling pathway is UDP-sugar pyrophosphorylase (USP), a single copy gene in Arabidopsis, of which a knockout is lethal for pollen development. Here we analyze the dependency between USP enzyme activity and the upstream glucuronokinase. Gene silencing of USP by miRNA cause a concomitant reduction of USP and of glucuronokinase activity presumably to prevent the accumulation of sugar-1-phosphates interfering with normal metabolism and depleting the phosphate pool of the cell. Landes Bioscience 2013-09-01 2013-06-28 /pmc/articles/PMC4002622/ /pubmed/23857351 http://dx.doi.org/10.4161/psb.25478 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Short Communication Geserick, Claudia Tenhaken, Raimund UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title | UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title_full | UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title_fullStr | UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title_full_unstemmed | UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title_short | UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
title_sort | udp-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4002622/ https://www.ncbi.nlm.nih.gov/pubmed/23857351 http://dx.doi.org/10.4161/psb.25478 |
work_keys_str_mv | AT geserickclaudia udpsugarpyrophosphorylasecontrolstheactivityofproceedingsugar1kinasesenzymes AT tenhakenraimund udpsugarpyrophosphorylasecontrolstheactivityofproceedingsugar1kinasesenzymes |