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1.
Environ Entomol ; 37(2): 586-91, 2008 Apr.
Article in English | MEDLINE | ID: mdl-18419932

ABSTRACT

Greenbug, Schizaphis graminum (Rondani) (Hemiptera: Aphididae), was first discovered damaging seashore paspalum (Paspalum vaginatum Swartz) turfgrass in November 2003 at Belle Glade, FL. Inquiries to several golf courses with seashore paspalum turf across southern Florida indicated infestation was wide spread by April 2004. Damage symptoms progress from water soaked lesions surrounding feeding sites within 24 h to chlorosis and necrosis of leaf tips within 96 h. Problems caused by greenbug feeding were initially misdiagnosed as fertilizer, disease, other insects, or water management problems because aphids were not previously found on warm season turfgrasses. Greenbug development and fecundity studies were conducted on six seashore paspalum varieties: 'Aloha,' 'SeaDwarf,' 'SeaGreen,' 'SeaIsle,' 'SeaWay,' and 'SeaWolf.' Greenbug did not survive on 'SeaWolf.' Development rates (mean +/- SEM) ranged from 7.6 +/- 0.2 to 8.2 +/- 0.2 d on the remaining varieties. Greenbug longevity and fecundity on 'Aloha' were significantly less than on the other varieties. The estimated intrinsic rate of natural increase (r(m)) for greenbug ranged from 0.24 to 0.26 across tested varieties. Values for net reproductive rate (R(o)) ranged from 12.3 on 'Aloha' to 40.4 on 'SeaWay.' In feeding trials on indicator plants, the Florida isolate of greenbug exhibited a unique biotypic profile most commonly found on noncultivated grass hosts. It was virulent on the wheat variety GRS1201 that is resistant to the principal agricultural biotypes attacking small grains and to all currently available resistant sorghum varieties.


Subject(s)
Aphids/classification , Aphids/physiology , Paspalum/parasitology , Aging , Animals , Ecosystem , Female , Reproduction/physiology
2.
Poult Sci ; 83(1): 15-23, 2004 Jan.
Article in English | MEDLINE | ID: mdl-14761079

ABSTRACT

Two commercial strains, Hy-Line W-36 and DeKalb XL, were moved to a laying house at 18 wk of age. They were housed 6 hens/layer cage at 2 densities (361 and 482 cm2/bird) with 2 replications each per strain/density combination. The high-density treatment contained 24 hens/replication and the low-density treatment contained 18 hens/replication for a total of 168 hens. Production parameters were measured during the first egg production cycle, the molt period, and the first 4 wk of the second lay cycle (20 to 68 wk of age). Behavioral observations were taken during 2 consecutive d at 26, 34, 43, 51, 62, 64, and 68 wk of age to examine behavioral patterns. Modified Hansen's tests were conducted concurrently to provide indication of the fearfulness levels of hens at the various stages of production. The production characteristics were similar for both strains. The hens kept at the higher density had lower (P < 0.01) hen-day production and (P < 0.05) daily egg mass. Appetitive behaviors were not affected by strain or density but were affected by the age of the hen and by molting. During the molt, feeding and drinking behavioral acts were fewer (P < 0.05) at 0.018 and 0.013 acts per bird/min, respectively, and standing behavior was highest. The results indicated that the frequencies of pecking inedible objects during the molt period were similar to the frequencies at 26 and 34 wk. Hens performed more acts of standing, and crouching and had lower frequency of movement during the molt. Those kept at a low density performed more movement acts. Feather pecking decreased as hens aged and increased when they molted but was not affected by strain or density. The frequency of aggression and submissive acts was significantly lower during the molt period. Behaviors were affected by strain, density, bird age, and molting; however, the patterns and number of aggressive acts did not increase to compromise the welfare status of the hens. Behaviors during the molt appeared consistent with mechanisms for conservation of body reserves.


Subject(s)
Behavior, Animal , Chickens/physiology , Housing, Animal , Molting/physiology , Age Factors , Aging/physiology , Animal Husbandry/methods , Animal Welfare , Animals , Feathers/injuries , Female , Oviposition/physiology , Population Density , Random Allocation
3.
Proc Natl Acad Sci U S A ; 98(22): 12578-83, 2001 Oct 23.
Article in English | MEDLINE | ID: mdl-11675494

ABSTRACT

In addition to its well-established role in responding to phosphate starvation, the cyclin-dependent kinase Pho85 has been implicated in a number of other physiological responses of the budding yeast Saccharomyces cerevisiae, including synthesis of glycogen. To comprehensively characterize the range of Pho85-dependent gene expression, we used a chemical genetic approach that enabled us to control Pho85 kinase activity with a cell-permeable inhibitor and whole genome transcript profiling. We found significant phenotypic differences between the rapid loss of activity caused by inhibition and the deletion of the genomic copy of PHO85. We demonstrate that Pho85 controls the expression of not only previously identified glycogen synthetic genes, but also a significant regulon of genes involved in the cellular response to environmental stress. In addition, we show that the effects of this inhibitor are both rapid and reversible, making it well suited to the study of the behavior of dynamic signaling pathways.


Subject(s)
Cyclin-Dependent Kinases/physiology , Enzyme Inhibitors/pharmacology , Saccharomyces cerevisiae Proteins/physiology , Alleles , Cyclin-Dependent Kinases/antagonists & inhibitors , Cyclin-Dependent Kinases/genetics , Environment , Gene Expression Regulation , Oligonucleotide Array Sequence Analysis , Saccharomyces cerevisiae Proteins/antagonists & inhibitors , Saccharomyces cerevisiae Proteins/genetics
4.
Poult Sci ; 79(4): 514-8, 2000 Apr.
Article in English | MEDLINE | ID: mdl-10780646

ABSTRACT

Two commercial strains of 18-wk-old Single Comb White Leghorn (SCWL) hens, HyLine W-36 and DeKalb XL, were housed six hens per cage in layer cages at two densities (361 and 482 cm2 per bird) with two replications each per strain and density combination. The high density treatment contained 24 hens per replication, and the low density treatment contained 18 hens per replication. Egg production was measured during the first egg production cycle, a molt (fast) period, and the first 4 wk of the second lay cycle (20 to 68 wk of age). Blood samples were obtained from six hens from each replicate in each strain and density combination (total of 48) at 20, 26, 34, 43, 51, 62, 64, and 68 wk of age. In addition, blood samples were obtained in a random order from hens in each cage, and the sequence of sampling was recorded (1 to 6). Blood smears were made, from which heterophil to lymphocyte ratios (H:L) were determined. Radioimmunoassays were conducted to determine levels of plasma corticosterone (CS), 3,5,3'-triiodothyronine (T3), and thyroxine (T4). The results indicated that strain did not affect percentage hen-day egg production (%HDP). Strain and cage density did not affect H:L, T3, T4, or CS. However, these parameters were affected by bird age, which was related to the egg production cycle. Plasma CS significantly (P < or = 0.001) increased during peak %HDP at 26 wk and 64 wk during the molt (fast), and H:L significantly (P < or = 0.001) increased during the molt (fast) at 64 wk. The sequence in which blood samples were obtained, from hens within a cage in sampling order, also increased plasma CS. The CS was significantly (P < or = 0.001) elevated in the third, fifth, and sixth hens from which blood samples were drawn. Plasma T3 and T4 changed during the production cycle. The T3 was significantly (P < or = 0.0001) depressed during peak egg production at 26 wk and during the molt (fast) at 64 wk when compared with the other time periods. Plasma T4 was depressed (P < or = 0.0001) at 51 wk and was elevated (P < or = 0.0001) at 64 wk during the molt (fast). The physiological and metabolic parameters of the different hen strains and cage densities were similar during egg production. However, CS, T3, T4, and H:L changed with age in relation to the egg production cycle. In addition, the physiological demands of peak egg production and molt (fast) appeared to be similar.


Subject(s)
Chickens/physiology , Corticosterone/blood , Housing, Animal , Leukocyte Count , Lymphocyte Count , Molting , Thyroid Hormones/blood , Aging , Animals , Female , Oviposition , Thyroxine/blood , Triiodothyronine/blood
5.
Mol Cell Biol ; 19(4): 3039-50, 1999 Apr.
Article in English | MEDLINE | ID: mdl-10082571

ABSTRACT

The Caenorhabditis elegans SKN-1 protein binds DNA through a basic region like those of bZIP proteins and through a flexible amino-terminal arm segment similar to those with which numerous helix-turn-helix proteins bind to bases in the minor groove. A recent X-ray crystallographic structure suggests that the SKN-1 amino-terminal arm provides only nonspecific DNA binding. In this study, however, we demonstrate that this segment mediates recognition of an AT-rich element that is part of the preferred SKN-1 binding site and thereby significantly increases the sequence specificity with which SKN-1 binds DNA. Mutagenesis experiments show that multiple amino acid residues within the arm are involved in binding. These residues provide binding affinity through distinct but partially redundant interactions and enhance specificity by discriminating against alternate sites. The AT-rich element minor groove is important for binding of the arm, which appears to affect DNA conformation in this region. This conformational effect does not seem to involve DNA bending, however, because the arm does not appear to affect a modest DNA bend that is induced by SKN-1. The data illustrate an example of how a small, flexible protein segment can make an important contribution to DNA binding specificity through multiple interactions and mechanisms.


Subject(s)
Caenorhabditis elegans Proteins , DNA-Binding Proteins/metabolism , Helminth Proteins/metabolism , Transcription Factors/metabolism , Adenine , Amino Acid Sequence , Animals , Binding Sites , Caenorhabditis elegans , DNA Probes , DNA-Binding Proteins/genetics , Helminth Proteins/genetics , Models, Molecular , Molecular Sequence Data , Mutation , Nucleic Acid Conformation , Protein Binding , Sequence Deletion , Thymine , Transcription Factors/genetics
6.
Genes Dev ; 11(17): 2227-38, 1997 Sep 01.
Article in English | MEDLINE | ID: mdl-9303538

ABSTRACT

The SKN-1 transcription factor specifies early embryonic cell fates in Caenorhabditis elegans. SKN-1 binds DNA at high affinity as a monomer, by means of a basic region like those of basic-leucine zipper (bZIP) proteins, which bind DNA only as dimers. We have investigated how the SKN-1 DNA-binding domain (the Skn domain) promotes stable binding of a basic region monomer to DNA. A flexible arm at the Skn domain amino terminus binds in the minor groove, but a support segment adjacent to the carboxy-terminal basic region can independently stabilize basic region-DNA binding. Off DNA, the basic region and arm are unfolded and, surprisingly, the support segment forms a molten globule of four alpha-helices. On binding DNA, the Skn domain adopts a tertiary structure in which the basic region helix extends directly from a support segment alpha-helix, which is required for binding. The remainder of the support segment anchors this uninterrupted helix on DNA, but leaves the basic region exposed in the major groove. This is similar to how the bZIP basic region extends from the leucine zipper, indicating that positioning and cooperative stability provided by helix extension are conserved mechanisms that promote binding of basic regions to DNA.


Subject(s)
Caenorhabditis elegans Proteins , DNA-Binding Proteins , DNA/metabolism , Helminth Proteins/chemistry , Helminth Proteins/metabolism , Transcription Factors/chemistry , Transcription Factors/metabolism , Amino Acid Sequence , Animals , Base Sequence , Binding Sites/genetics , Caenorhabditis elegans/embryology , Caenorhabditis elegans/genetics , Caenorhabditis elegans/metabolism , DNA/chemistry , Helminth Proteins/genetics , Magnetic Resonance Spectroscopy , Models, Molecular , Molecular Sequence Data , Mutagenesis, Site-Directed , Nucleic Acid Conformation , Protein Folding , Protein Structure, Secondary , Transcription Factors/genetics
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