| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Yang, Wenqiang Catalanotti, Claudia D'Adamo, Sarah Wittkopp, Tyler M. Ingram-Smith, Cheryl J. Mackinder, Luke Miller, Tarryn E. Heuberger, Adam L. Peers, Graham Smith, Kerry S. Jonikas, Martin C. Grossman, Arthur R. Posewitz, Matthew C. |
| Description |
Author Affiliation: Yang W ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305 wqyang@stanford.edu.); Catalanotti C ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305.); D'Adamo S ( Colorado School of Mines, Department of Chemistry and Geochemistry, Golden, Colorado 80401.); Wittkopp TM ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305 Stanford University, Department of Biology, Stanford, California 94305.); Ingram-Smith CJ ( Clemson University, Department of Genetics and Biochemistry, Clemson, South Carolina 29634.); Mackinder L ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305.); Miller TE ( Colorado School of Mines, Department of Chemistry and Geochemistry, Golden, Colorado 80401.); Heuberger AL ( Colorado State University, Proteomics and Metabolomics Facility, Fort Collins, Colorado 80523.); Peers G ( Colorado State University, Department of Biology, Fort Collins, Colorado 80523.); Smith KS ( Clemson University, Department of Genetics and Biochemistry, Clemson, South Carolina 29634.); Jonikas MC ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305.); Grossman AR ( Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305.); Posewitz MC ( Colorado School of Mines, Department of Chemistry and Geochemistry, Golden, Colorado 80401.) |
| Abstract |
Chlamydomonas reinhardtii insertion mutants disrupted for genes encoding acetate kinases (EC 2.7.2.1) (ACK1 and ACK2) and a phosphate acetyltransferase (EC 2.3.1.8) (PAT2, but not PAT1) were isolated to characterize fermentative acetate production. ACK1 and PAT2 were localized to chloroplasts, while ACK2 and PAT1 were shown to be in mitochondria. Characterization of the mutants showed that PAT2 and ACK1 activity in chloroplasts plays a dominant role (relative to ACK2 and PAT1 in mitochondria) in producing acetate under dark, anoxic conditions and, surprisingly, also suggested that Chlamydomonas has other pathways that generate acetate in the absence of ACK activity. We identified a number of proteins associated with alternative pathways for acetate production that are encoded on the Chlamydomonas genome. Furthermore, we observed that only modest alterations in the accumulation of fermentative products occurred in the ack1, ack2, and ack1 ack2 mutants, which contrasts with the substantial metabolite alterations described in strains devoid of other key fermentation enzymes. |
| File Format |
HTM / HTML |
| ISSN |
10404651 |
| e-ISSN |
1531298X |
| DOI |
10.1105/tpc.114.129965 |
| Journal |
THE PLANT CELL ONLINE |
| Issue Number |
11 |
| Volume Number |
26 |
| Language |
English |
| Publisher |
American Society of Plant Biologists |
| Publisher Date |
2014-11-01 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Discipline Botany Acetate Kinase Metabolism Acetates Chlamydomonas Reinhardtii Enzymology Chloroplasts Phosphate Acetyltransferase Genetics Algal Proteins Fermentation Mitochondria Mutagenesis, Insertional Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Plant Science |
