Dynamic proteomic profiling of a unicellular cyanobacterium Cyanothece ATCC51142 across light-dark diurnal cycles

Journal Article · Thu Dec 01 00:00:00 EST 2011 · BMC Systems Biology, 5:Article No. 194

DOI:https://doi.org/10.1186/1752-0509-5-194· OSTI ID:1036420

Aryal, Uma K; Stockel, Jana; Krovvidi, Ravi K; Gritsenko, Marina A; Monroe, Matthew E; Moore, Ronald J; Koppenaal, David W; Smith, Richard D; Pakrasi, Himadri B; Jacobs, Jon M

Unicellular cyanobacteria of the genus Cyanothece are recognized for their ability to execute nitrogen (N2)-fixation in the dark and photosynthesis in the light. Systems-wide dynamic proteomic profiling with mass spectrometry (MS) analysis reveals fundamental insights into the control and regulation of these functions. To expand upon the current knowledge of protein expression patterns in Cyanothece ATCC51142, we performed quantitative proteomic analysis using partial ("unsaturated") metabolic labeling and high mass accuracy LC-MS analysis. This dynamic proteomic profiling identified 721 actively synthesized proteins with significant temporal changes in expression throughout the light-dark cycles, of which 425 proteins matched with previously characterized cycling transcripts. The remaining 296 proteins contained a cluster of proteins uniquely involved in DNA replication and repair, protein degradation, tRNA synthesis and modification, transport and binding, and regulatory functions. Analysis of protein functions revealed that the expression of nitrogenase in the dark is mediated by higher respiration and glycogen metabolism. We have also shown that Cyanothece ATCC51142 utilizes alternative pathways for carbon (C) and nitrogen (N) acquisition, particularly, aspartic acid and glutamate as substrates of C and N, respectively. Utilization of phosphoketolase (PHK) pathway for the conversion of xylulose-5P to pyruvate and acetyl-P likely constitutes an alternative strategy to compensate higher ATP and NADPH demand. In conclusion, this study provides a deeper insight into how Cyanothece ATCC51142 modulates cellular functions to accommodate photosynthesis and N2-fixation within the single cell.

• Research Organization: Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 1036420
• Report Number(s): PNNL-SA-81418; 16720; TRN: US201206%%293
• Journal Information: BMC Systems Biology, 5:Article No. 194, Vol. 5
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
ACCURACY
ASPARTIC ACID
CARBON
CYANOBACTERIA
DNA REPLICATION
GLYCOGEN
MASS SPECTROSCOPY
METABOLISM
NITROGEN
NITROGENASE
PHOTOSYNTHESIS
PROTEINS
REGULATIONS
REPAIR
RESPIRATION
SUBSTRATES
SYNTHESIS
TRANSPORT
protein expression dynamics in Cyanothece ATCC51142
SP STRAIN ATCC-51142
MASS-SPECTROMETRY
PROTEIN-TURNOVER
DIAZOTROPHIC CYANOBACTERIUM
ATCC 51142
EXPRESSION
SYNECHOCYSTIS
FIXATION
PATHWAY
Environmental Molecular Sciences Laboratory