Characterization of Two Acetyl-CoA Carboxylase Isoforms in Diclofop-Methyl-Resistant and -Susceptible Biotypes of Alopecurus myosuroides

1999 ◽  
Vol 65 (2) ◽  
pp. 82-89 ◽  
Author(s):  
Julio Menéndez ◽  
Rafael De Prado
Keyword(s):  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Alopecurus Myosuroides

Characterization of cross-resistance patterns in acetyl-CoA carboxylase inhibitor resistant wild oat (Avena fatua)

Weed Science ◽  
1997 ◽  
Vol 45 (6) ◽  
pp. 750-755 ◽  
Author(s):  
Luc Bourgeois ◽  
Norm C. Kenkel ◽  
Ian N. Morrison
Keyword(s):  
Cluster Analysis ◽  
Principal Component ◽  
Petri Dish ◽  
Cross Resistance ◽  
Wild Oat ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pairwise Correlation ◽  
Resistance Patterns

The purpose of this study was to determine cross-resistance patterns among wild oat lines resistant to acetyl-CoA carboxylase (ACCase) inhibitors and to determine which, if any, cross-resistant type was more common than another. Discriminatory concentrations of two aryloxyphenoxy-propionates (APP) and three cyclohexanediones (CHD) were determined using a petri-dish bioassay. These concentrations were then applied to 82 resistant wild oat lines identified in previous studies. In addition, two resistant standards (UM1 and UM33) and a susceptible standard (UM5) were included in the experiments. Coleoptile lengths expressed as percentages of untreated controls were used to assess the level of resistance to each herbicide. Large variations were observed among wild oat lines and herbicides. However, cluster analysis summarized the relationship between the five herbicides (variables) and the wild oat lines into three main cross-resistance types. Type A included wild oat lines with high resistance to APP herbicides and no or low resistance to CHD herbicides. Types B and C included those with low to moderate resistant and high levels of resistance to all five herbicides, respectively. Type C was the most common cross-resistance type. Relationships among herbicides were determined using pairwise correlation and principal component analysis (PCA). All correlations were high between APP herbicides and between CHD herbicides but not between APP and CHD herbicides. The first two axes of the PCA accounted for 88.4% of the total variance, with the first axis correlated to the CHD herbicides and the second axis correlated to the APP herbicides. In the PCA, wild oat lines were segregated into the three types identified in the cluster analysis. Although CHD and APP herbicides bind at the same region on the ACCase, resistant wild oat lines respond differently to them.

scholarly journals Localization and characterization of two structurally different forms of acetyl-CoA carboxylase in young pea leaves, of which one is sensitive to aryloxyphenoxypropionate herbicides

1994 ◽  
Vol 300 (2) ◽  
pp. 557-565 ◽  
Author(s):  
C Alban ◽  
P Baldet ◽  
R Douce
Keyword(s):  
Molecular Mass ◽  
Subunit Structure ◽  
Acetyl Coa Carboxylase ◽  
Leaf Extracts ◽  
Acetyl Coa ◽  
Native Molecular Mass ◽  
Molecular Masses ◽  
Minor Form ◽  
A Minor

Young pea leaves contain two structurally different forms of acetyl-CoA carboxylase (EC 6.4.1.2; ACCase). A minor form, which accounted for about 20% of the total ACCase activity in the whole leaf, was detected in the epidermal tissue. This enzyme was soluble and was purified to homogeneity from young pea leaf extracts. It consisted of a dimer of two identical biotinyl subunits of molecular mass 220 kDa. In this respect, this multifunctional enzyme was comparable with that described in other plants and in other eukaryotes. A predominant form was present in both the epidermal and mesophyll tissues. In mesophyll protoplasts, ACCase was detected exclusively in the soluble phase of chloroplasts. This enzyme was partially purified from pea chloroplasts and consisted of a freely dissociating complex, the activity of which may be restored by combination of its separated constituents. The partially purified enzyme was composed of several subunits of molecular masses ranging from 32 to 79 kDa, for a native molecular mass > 600 kDa. One of these subunits, of molecular mass 38 kDa, was biotinylated. This complex subunit structure was comparable with that of microorganisms and was referred to as a ‘prokaryotic’ form of ACCase. Biochemical parameters were determined for both ACCase forms. Finally, both pea leaf ACCases exhibited different sensitivities towards the grass ACCase herbicide, diclofop. This compound had no effect on the ‘prokaryotic’ form of ACCase, while the ‘eukaryotic’ form was strongly inhibited.

Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics

2009 ◽  
Vol 1794 (6) ◽  
pp. 961-967 ◽  
Author(s):  
Virendar K. Kaushik ◽  
Michael Kavana ◽  
Jessica M. Volz ◽  
Stephen C. Weldon ◽  
Susan Hanrahan ◽  
...  
Keyword(s):  
Steady State ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Steady State Kinetics

Expression, purification, and characterization of human acetyl-CoA carboxylase 2

2007 ◽  
Vol 53 (1) ◽  
pp. 16-23 ◽  
Author(s):  
Ki Won Kim ◽  
Harvey Yamane ◽  
James Zondlo ◽  
James Busby ◽  
Minghan Wang
Keyword(s):  
Acetyl Coa Carboxylase ◽  
Purification And Characterization ◽  
Acetyl Coa
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