Quantification of protein copy number in yeast: the NAD+ metabolome.

Saccharomyces cerevisiae is calorie-restricted by lowering glucose from 2% to 0.5%. Under low glucose conditions, replicative lifespan is extended in a manner that depends on the NAD+-dependent protein lysine deacetylase Sir2 and NAD+ salvage enzymes. Because NAD+ is required for glucose utilization...

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Autores principales:	Szu-Chieh Mei, Charles Brenner
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e95f003c144a47c0a83cde7bb1000ecb
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spelling	oai:doaj.org-article:e95f003c144a47c0a83cde7bb1000ecb2021-11-25T06:01:53ZQuantification of protein copy number in yeast: the NAD+ metabolome.1932-620310.1371/journal.pone.0106496https://doaj.org/article/e95f003c144a47c0a83cde7bb1000ecb2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25188219/?tool=EBIhttps://doaj.org/toc/1932-6203Saccharomyces cerevisiae is calorie-restricted by lowering glucose from 2% to 0.5%. Under low glucose conditions, replicative lifespan is extended in a manner that depends on the NAD+-dependent protein lysine deacetylase Sir2 and NAD+ salvage enzymes. Because NAD+ is required for glucose utilization and Sir2 function, it was postulated that glucose levels alter the levels of NAD+ metabolites that tune Sir2 function. Though NAD+ precursor vitamins, which increase the levels of all NAD+ metabolites, can extend yeast replicative lifespan, glucose restriction does not significantly change the levels or ratios of intracellular NAD+ metabolites. To test whether glucose restriction affects protein copy numbers, we developed a technology that combines the measurement of Urh1 specific activity and quantification of relative expression between Urh1 and any other protein. The technology was applied to obtain the protein copy numbers of enzymes involved in NAD+ metabolism in rich and synthetic yeast media. Our data indicated that Sir2 and Pnc1, two enzymes that sequentially convert NAD+ to nicotinamide and then to nicotinic acid, are up-regulated by glucose restriction in rich media, and that Pnc1 alone is up-regulated in synthetic media while levels of all other enzymes are unchanged. These data suggest that production or export of nicotinic acid might be a connection between NAD+ and calorie restriction-mediated lifespan extension in yeast.Szu-Chieh MeiCharles BrennerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e106496 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Szu-Chieh Mei Charles Brenner Quantification of protein copy number in yeast: the NAD+ metabolome.
description	Saccharomyces cerevisiae is calorie-restricted by lowering glucose from 2% to 0.5%. Under low glucose conditions, replicative lifespan is extended in a manner that depends on the NAD+-dependent protein lysine deacetylase Sir2 and NAD+ salvage enzymes. Because NAD+ is required for glucose utilization and Sir2 function, it was postulated that glucose levels alter the levels of NAD+ metabolites that tune Sir2 function. Though NAD+ precursor vitamins, which increase the levels of all NAD+ metabolites, can extend yeast replicative lifespan, glucose restriction does not significantly change the levels or ratios of intracellular NAD+ metabolites. To test whether glucose restriction affects protein copy numbers, we developed a technology that combines the measurement of Urh1 specific activity and quantification of relative expression between Urh1 and any other protein. The technology was applied to obtain the protein copy numbers of enzymes involved in NAD+ metabolism in rich and synthetic yeast media. Our data indicated that Sir2 and Pnc1, two enzymes that sequentially convert NAD+ to nicotinamide and then to nicotinic acid, are up-regulated by glucose restriction in rich media, and that Pnc1 alone is up-regulated in synthetic media while levels of all other enzymes are unchanged. These data suggest that production or export of nicotinic acid might be a connection between NAD+ and calorie restriction-mediated lifespan extension in yeast.
format	article
author	Szu-Chieh Mei Charles Brenner
author_facet	Szu-Chieh Mei Charles Brenner
author_sort	Szu-Chieh Mei
title	Quantification of protein copy number in yeast: the NAD+ metabolome.
title_short	Quantification of protein copy number in yeast: the NAD+ metabolome.
title_full	Quantification of protein copy number in yeast: the NAD+ metabolome.
title_fullStr	Quantification of protein copy number in yeast: the NAD+ metabolome.
title_full_unstemmed	Quantification of protein copy number in yeast: the NAD+ metabolome.
title_sort	quantification of protein copy number in yeast: the nad+ metabolome.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/e95f003c144a47c0a83cde7bb1000ecb
work_keys_str_mv	AT szuchiehmei quantificationofproteincopynumberinyeastthenadmetabolome AT charlesbrenner quantificationofproteincopynumberinyeastthenadmetabolome
_version_	1718414313551560704

Quantification of protein copy number in yeast: the NAD+ metabolome.

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