|
1.
|
gene
AT1G64710.1 ( pub:1781)
Alias:
F13O11.3 | F13O11_3
TAIR:gene:2010810 (Accession)
|
Article [ 23892 ]
(1995)
[research_article]
Aerobic fermentation in tobacco pollen.
(PDF)
PLANT MOLECULAR BIOLOGY
Bucher,M.,Brander,K.A.,Sbicego,S.,Mandel,T.,Kuhlemeier,C.
(TAIR Reference:501683241)
We characterized the genes coding for the two dedicated enzymes of ethanolic fermentation, alcohol dehydrogenase (ADH) and pyruvate decarboxylase (PDC), and show that they are functional in pollen. Two PDC-encoding genes were isolated, which displayed reciprocal regulation: PDC1 was anaerobically induced in leaves, whereas PDC2 mRNA was absent in leaves, but constitutively present in pollen. A flux through the ethanolic fermentation pathway could be measured in pollen under all tested environmental and developmental conditions. Surprisingly, the major factor influencing the rate of ethanol production was not oxygen availability, but the composition of the incubation medium. Under optimal conditions for pollen tube growth, approximately two-thirds of the carbon consumed was fermented, and ethanol accumulated into the surrounding medium to a concentration exceeding 100 mM.
Scanned By: garcia
Other associated terms:
alcohol dehydrogenase (NAD+) activity /
pyruvate decarboxylase activity /
fermentation /
AT1G64710.1 /
growth /
pollen tube growth /
AT1G77120 (ADH1) /
AT4G33070 (PDC1) /
AT5G54960 (PDC2) /
pollen tube /
pollen /
|
Searched on
|
|
|
2.
|
gene
AT1G64710.1 ( pub:1781)
Alias:
F13O11.3 | F13O11_3
TAIR:gene:2010810 (Accession)
|
Article [ 86275 ]
(2017)
[research_article]
Analysis of protein complexes in Arabidopsis leaves using size exclusion chromatography and label-free protein correlation profiling
(PDF)
Journal of proteomics
Aryal, U. K., McBride, Z., Chen, D., Xie, J., Szymanski, D. B.
(TAIR Reference:501776000)
Protein complexes are fundamentally important for diverse cellular functions, and create functionalities that could never be achieved by a single polypeptide. Knowledge of the protein complex assemblies that exist in plant cells are limited. To close this gap, we applied an integrative proteomic approach that combines cell fractionation, protein chromatography and quantitative mass spectrometry (MS) to analyze the oligomerization state of thousands of proteins in a single experiment. Soluble extracts from intact Arabidopsis leaves were fractionated using size exclusion chromatography (SEC), and abundance profiles across the column fractions were quantified using label-free precursor ion (MS1) intensity. In duplicate experiments, we reproducibly detected 1693 proteins, of which 983 proteins were cytosolic. Based on the SEC profiles, approximately one third of all of the soluble proteins were predicted to be oligomeric. Our dataset includes both subunits of previously known complexes as well as hundreds of new protein complexes. The label-free MS1-based quantification method described here produced a highly useful dataset for the plant biology community, and provided a foundation to incorporate orthogonal protein complex separation methods so the composition and dynamics of protein complexes can be analyzed based on LC/MS profile data alone.
Not Scanned
Other associated terms:
protein binding /
AT1G14810.1 /
AT1G49820.1 /
AT1G07240.1 /
AT1G07040.1 /
AT1G07080.1 /
AT1G07250.1 /
AT1G07140.1 /
AT1G03030.1 /
AT1G51360.1 /
AT1G35420.1 /
AT1G67550.1 /
AT1G12050.1 /
AT1G11870.1 /
AT1G12010.1 /
AT1G12000.1 /
AT1G11910.1 /
AT1G06570.1 /
AT1G06550.1 /
AT1G22400.1 /
AT1G53240.1 /
AT1G53280.1 /
AT1G65970.1 /
AT1G65980.1 /
AT1G65930.1 /
AT1G30230.1 /
AT1G42970.1 /
AT1G12780.1 /
AT1G27950.1 /
AT1G27970.1 /
AT1G56450.1 /
AT1G56500.1 /
AT1G64980.1 /
AT1G64710.1 /
AT1G19130.1 /
AT1G35720.1 /
AT1G50320.1 /
AT1G50200.1 /
AT1G50380.1 /
AT1G49650.1 /
AT1G49660.1 /
AT1G09620.1 /
AT1G09490.1 /
AT1G09430.1 /
AT1G68760.1 /
AT1G20340.1 /
AT1G71840.1 /
AT1G71730.1 /
AT1G36280.1 /
AT1G29660.1 /
... (1652 other terms not shown)
|
Searched on 2019-01-09
|
|