Natural osmolytes are much less effective substrates than glycogen for catabolic energy production in the marine cyanobacterium Synechococcus sp. strain PCC 7002

L. Tiago Guerra, Yu Xu, Nicholas Bennette, Kelsey McNeely, Donald A. Bryant, G Charles Dismukes

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

ADP-glucose pyrophosphorylase, encoded by glgC, catalyzes the first step of glycogen and glucosylglycer(ol/ate) biosynthesis. Here we report the construction of the first glgC null mutant of a marine cyanobacterium ( Synechococcus sp. PCC 7002) and investigate its impact on dark anoxic metabolism (autofermentation). The glgC mutant had 98% lower ADP-glucose, synthesized no glycogen and produced appreciably more soluble sugars (mainly sucrose) than wild type (WT). Some glucosylglycerol was still observed, which suggests that the mutant has another, inefficient ADP-glucose synthesis pathway. In contrast, hypersaline conditions (1. M NaCl) were lethal to the mutant strain, indicating that, unlike other strains, the elevated sucrose does not compensate for the reduced GG as osmolyte. In contrast to WT, nitrate limitation did not cause bleaching of N-containing pigments or carbohydrate accumulation in the glgC mutant, indicating impaired recycling of nitrogen stores. Despite the 2-fold increase in osmolytes, both the respiration and autofermentation rates of the glgC mutant were appreciably slower (2-4-fold) and correlated quantitatively with the lower fraction of insoluble carbohydrates relative to WT (85% vs. 12%). However, the remaining insoluble carbohydrates still accounted for a high fraction of the carbohydrate catabolized (38%), indicating that insoluble carbohydrates rather than osmolytes were the preferred substrate for autofermentation.

Original languageEnglish
Pages (from-to)65-75
Number of pages11
JournalJournal of Biotechnology
Volume166
Issue number3
DOIs
Publication statusPublished - Jul 2013

Fingerprint

Synechococcus
Cyanobacteria
Carbohydrates
Glycogen
Administrative data processing
Sugar (sucrose)
Adenosine Diphosphate Glucose
Glucose
Substrates
Sucrose
Glucose-1-Phosphate Adenylyltransferase
Biosynthesis
Respiratory Rate
Bleaching
Metabolism
Pigments
Sugars
Nitrates
Recycling
Nitrogen

Keywords

  • ADP-glucose pyrophosphorylase
  • Autofermentation
  • Cyanobacteria
  • Glycogen
  • Osmolytes
  • Stress Conditions

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Natural osmolytes are much less effective substrates than glycogen for catabolic energy production in the marine cyanobacterium Synechococcus sp. strain PCC 7002. / Guerra, L. Tiago; Xu, Yu; Bennette, Nicholas; McNeely, Kelsey; Bryant, Donald A.; Dismukes, G Charles.

In: Journal of Biotechnology, Vol. 166, No. 3, 07.2013, p. 65-75.

Research output: Contribution to journalArticle

@article{a7e8e97a2ef54b01ab9455c91ad68bf9,
title = "Natural osmolytes are much less effective substrates than glycogen for catabolic energy production in the marine cyanobacterium Synechococcus sp. strain PCC 7002",
abstract = "ADP-glucose pyrophosphorylase, encoded by glgC, catalyzes the first step of glycogen and glucosylglycer(ol/ate) biosynthesis. Here we report the construction of the first glgC null mutant of a marine cyanobacterium ( Synechococcus sp. PCC 7002) and investigate its impact on dark anoxic metabolism (autofermentation). The glgC mutant had 98{\%} lower ADP-glucose, synthesized no glycogen and produced appreciably more soluble sugars (mainly sucrose) than wild type (WT). Some glucosylglycerol was still observed, which suggests that the mutant has another, inefficient ADP-glucose synthesis pathway. In contrast, hypersaline conditions (1. M NaCl) were lethal to the mutant strain, indicating that, unlike other strains, the elevated sucrose does not compensate for the reduced GG as osmolyte. In contrast to WT, nitrate limitation did not cause bleaching of N-containing pigments or carbohydrate accumulation in the glgC mutant, indicating impaired recycling of nitrogen stores. Despite the 2-fold increase in osmolytes, both the respiration and autofermentation rates of the glgC mutant were appreciably slower (2-4-fold) and correlated quantitatively with the lower fraction of insoluble carbohydrates relative to WT (85{\%} vs. 12{\%}). However, the remaining insoluble carbohydrates still accounted for a high fraction of the carbohydrate catabolized (38{\%}), indicating that insoluble carbohydrates rather than osmolytes were the preferred substrate for autofermentation.",
keywords = "ADP-glucose pyrophosphorylase, Autofermentation, Cyanobacteria, Glycogen, Osmolytes, Stress Conditions",
author = "Guerra, {L. Tiago} and Yu Xu and Nicholas Bennette and Kelsey McNeely and Bryant, {Donald A.} and Dismukes, {G Charles}",
year = "2013",
month = "7",
doi = "10.1016/j.jbiotec.2013.04.005",
language = "English",
volume = "166",
pages = "65--75",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Natural osmolytes are much less effective substrates than glycogen for catabolic energy production in the marine cyanobacterium Synechococcus sp. strain PCC 7002

AU - Guerra, L. Tiago

AU - Xu, Yu

AU - Bennette, Nicholas

AU - McNeely, Kelsey

AU - Bryant, Donald A.

AU - Dismukes, G Charles

PY - 2013/7

Y1 - 2013/7

N2 - ADP-glucose pyrophosphorylase, encoded by glgC, catalyzes the first step of glycogen and glucosylglycer(ol/ate) biosynthesis. Here we report the construction of the first glgC null mutant of a marine cyanobacterium ( Synechococcus sp. PCC 7002) and investigate its impact on dark anoxic metabolism (autofermentation). The glgC mutant had 98% lower ADP-glucose, synthesized no glycogen and produced appreciably more soluble sugars (mainly sucrose) than wild type (WT). Some glucosylglycerol was still observed, which suggests that the mutant has another, inefficient ADP-glucose synthesis pathway. In contrast, hypersaline conditions (1. M NaCl) were lethal to the mutant strain, indicating that, unlike other strains, the elevated sucrose does not compensate for the reduced GG as osmolyte. In contrast to WT, nitrate limitation did not cause bleaching of N-containing pigments or carbohydrate accumulation in the glgC mutant, indicating impaired recycling of nitrogen stores. Despite the 2-fold increase in osmolytes, both the respiration and autofermentation rates of the glgC mutant were appreciably slower (2-4-fold) and correlated quantitatively with the lower fraction of insoluble carbohydrates relative to WT (85% vs. 12%). However, the remaining insoluble carbohydrates still accounted for a high fraction of the carbohydrate catabolized (38%), indicating that insoluble carbohydrates rather than osmolytes were the preferred substrate for autofermentation.

AB - ADP-glucose pyrophosphorylase, encoded by glgC, catalyzes the first step of glycogen and glucosylglycer(ol/ate) biosynthesis. Here we report the construction of the first glgC null mutant of a marine cyanobacterium ( Synechococcus sp. PCC 7002) and investigate its impact on dark anoxic metabolism (autofermentation). The glgC mutant had 98% lower ADP-glucose, synthesized no glycogen and produced appreciably more soluble sugars (mainly sucrose) than wild type (WT). Some glucosylglycerol was still observed, which suggests that the mutant has another, inefficient ADP-glucose synthesis pathway. In contrast, hypersaline conditions (1. M NaCl) were lethal to the mutant strain, indicating that, unlike other strains, the elevated sucrose does not compensate for the reduced GG as osmolyte. In contrast to WT, nitrate limitation did not cause bleaching of N-containing pigments or carbohydrate accumulation in the glgC mutant, indicating impaired recycling of nitrogen stores. Despite the 2-fold increase in osmolytes, both the respiration and autofermentation rates of the glgC mutant were appreciably slower (2-4-fold) and correlated quantitatively with the lower fraction of insoluble carbohydrates relative to WT (85% vs. 12%). However, the remaining insoluble carbohydrates still accounted for a high fraction of the carbohydrate catabolized (38%), indicating that insoluble carbohydrates rather than osmolytes were the preferred substrate for autofermentation.

KW - ADP-glucose pyrophosphorylase

KW - Autofermentation

KW - Cyanobacteria

KW - Glycogen

KW - Osmolytes

KW - Stress Conditions

UR - http://www.scopus.com/inward/record.url?scp=84879210530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84879210530&partnerID=8YFLogxK

U2 - 10.1016/j.jbiotec.2013.04.005

DO - 10.1016/j.jbiotec.2013.04.005

M3 - Article

VL - 166

SP - 65

EP - 75

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 3

ER -