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Article: Maximizing soybean yield by understanding planting date, maturity group, and seeding rate interactions in North Carolina

Morris, Tristan C. / Vann, Rachel A. / Heitman, Josh / Collins, Guy D. / Heiniger, Ryan W.

Crop science. 2021 Nov., v. 61, no. 6

2021

Abstract: Growers across theU.S. Southeast use a diversity of soybean [Glycine max (L.) Merr.] planting dates, maturity groups, and seeding rates for soybean production depending on their rotational complexity. Studies were conducted across seven North Carolina ... ...

Abstract	Growers across theU.S. Southeast use a diversity of soybean [Glycine max (L.) Merr.] planting dates, maturity groups, and seeding rates for soybean production depending on their rotational complexity. Studies were conducted across seven North Carolina environments in 2019 and 2020 to determine the effect of planting date (mid‐March through mid‐July), maturity group (MG 2–8), and seeding rate (185,329–432,434 seeds ha–¹) on soybean emergence, stand, and yield. Across environments, soybean typically emerged more quickly with later planting dates; however, there were location‐specific variations in soybean emergence due to weather conditions around the time of planting. The longest and shortest emergence periods were 26 d for soybean planted in mid‐March and 4 d for soybean planted in June and July, respectively. In the higher yielding environments, yield was maximized with MG 3–4 cultivars planted at early April planting dates and yield declined as planting was delayed. In the low yield environments, yield was maximized with late April to mid‐May planting dates, typically with MG 5–7 cultivars. There was a penalty in both yield environments to planting past mid‐May and in the low yield environments for planting before mid‐April. Across environments, yields tended to be more similar among cultivars higher than MG 3 at planting dates in June and July. The effect of seeding rate on soybean yield was variable across planting dates, maturity groups, and yield environments. Future research is needed in North Carolina to validate the planting date and maturity group interactions on yield observed in this experiment to capture more variation in weather conditions.
Keywords	Glycine max ; cultivars ; soybeans ; weather ; North Carolina
Language	English
Dates of publication	2021-11
Size	p. 4365-4382.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	410209-5
ISSN	0011-183X
ISSN	0011-183X
DOI	10.1002/csc2.20603
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Infection of human mucosal tissue by Pseudomonas aeruginosa requires sequential and mutually dependent virulence factors and a novel pilus-associated adhesin.

Heiniger, Ryan W / Winther-Larsen, Hanne C / Pickles, Raymond J / Koomey, Michael / Wolfgang, Matthew C

Cellular microbiology

2010 Volume 12, Issue 8, Page(s) 1158–1173

Abstract: Tissue damage predisposes humans to life-threatening disseminating infection by the opportunistic pathogen Pseudomonas aeruginosa. Bacterial adherence to host tissue is a critical first step in this infection process. It is well established that P. ... ...

Abstract	Tissue damage predisposes humans to life-threatening disseminating infection by the opportunistic pathogen Pseudomonas aeruginosa. Bacterial adherence to host tissue is a critical first step in this infection process. It is well established that P. aeruginosa attachment to host cells involves type IV pili (TFP), which are retractile surface fibres. The molecular details of attachment and the identity of the bacterial adhesin and host receptor remain controversial. Using a mucosal epithelium model system derived from primary human tissue, we show that the pilus-associated protein PilY1 is required for bacterial adherence. We establish that P. aeruginosa preferentially binds to exposed basolateral host cell surfaces, providing a mechanistic explanation for opportunistic infection of damaged tissue. Further, we demonstrate that invasion and fulminant infection of intact host tissue requires the coordinated and mutually dependent action of multiple bacterial factors, including pilus fibre retraction and the host cell intoxication system, termed type III secretion. Our findings offer new and important insights into the complex interactions between a pathogen and its human host and provide compelling evidence that PilY1 serves as the principal P. aeruginosa adhesin for human tissue and that it specifically recognizes a host receptor localized or enriched on basolateral epithelial cell surfaces.
MeSH term(s)	Bacterial Adhesion ; Bacterial Toxins/genetics ; Bacterial Toxins/metabolism ; Cells, Cultured ; Epithelial Cells/microbiology ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/physiology ; Histocytochemistry ; Humans ; Microscopy ; Microscopy, Fluorescence ; Models, Biological ; Organ Culture Techniques ; Pseudomonas aeruginosa/pathogenicity ; Respiratory Mucosa/microbiology ; Virulence Factors/genetics ; Virulence Factors/metabolism
Chemical Substances	Bacterial Toxins ; PilY1 protein, Pseudomonas aeruginosa ; Virulence Factors ; Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2010-03-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/j.1462-5822.2010.01461.x
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Article: Infection of human mucosal tissue by Pseudomonas aeruginosa requires sequential and mutually dependent virulence factors and a novel pilus-associated adhesin

Heiniger, Ryan W / Winther-Larsen, Hanne C / Pickles, Raymond J / Koomey, Michael / Wolfgang, Matthew C

Cellular microbiology. 2010 Aug., v. 12, no. 8

2010

Abstract	Tissue damage predisposes humans to life-threatening disseminating infection by the opportunistic pathogen Pseudomonas aeruginosa. Bacterial adherence to host tissue is a critical first step in this infection process. It is well established that P. aeruginosa attachment to host cells involves type IV pili (TFP), which are retractile surface fibres. The molecular details of attachment and the identity of the bacterial adhesin and host receptor remain controversial. Using a mucosal epithelium model system derived from primary human tissue, we show that the pilus-associated protein PilY1 is required for bacterial adherence. We establish that P. aeruginosa preferentially binds to exposed basolateral host cell surfaces, providing a mechanistic explanation for opportunistic infection of damaged tissue. Further, we demonstrate that invasion and fulminant infection of intact host tissue requires the coordinated and mutually dependent action of multiple bacterial factors, including pilus fibre retraction and the host cell intoxication system, termed type III secretion. Our findings offer new and important insights into the complex interactions between a pathogen and its human host and provide compelling evidence that PilY1 serves as the principal P. aeruginosa adhesin for human tissue and that it specifically recognizes a host receptor localized or enriched on basolateral epithelial cell surfaces.
Language	English
Dates of publication	2010-08
Size	p. 1158-1173.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/j.1462-5822.2010.01461.x
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Article: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility

Orans, Jillian / Johnson, Michael D.L / Coggan, Kimberly A / Sperlazza, Justin R / Heiniger, Ryan W / Wolfgang, Matthew C / Redinbo, Matthew R

Proceedings of the National Academy of Sciences of the United States of America. 2010 Jan. 19, v. 107, no. 3

2010

Abstract: Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of ... ...

Abstract	Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 Ã resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified Î²-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner--by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility.
Keywords	Pseudomonas aeruginosa ; adenosinetriphosphatase ; calcium ; chelating agents ; crystal structure ; fimbriae ; human diseases ; lysine ; mutation ; pathogens
Language	English
Dates of publication	2010-0119
Size	p. 1065-1070.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0911616107
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Article ; Online: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility.

Orans, Jillian / Johnson, Michael D L / Coggan, Kimberly A / Sperlazza, Justin R / Heiniger, Ryan W / Wolfgang, Matthew C / Redinbo, Matthew R

Proceedings of the National Academy of Sciences of the United States of America

2009 Volume 107, Issue 3, Page(s) 1065–1070

Abstract	Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 A resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified beta-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner--by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility.
MeSH term(s)	Amino Acid Sequence ; Calcium/physiology ; Crystallography, X-Ray ; Fimbriae Proteins/chemistry ; Models, Molecular ; Protein Conformation ; Pseudomonas aeruginosa/chemistry ; Pseudomonas aeruginosa/physiology
Chemical Substances	PilY1 protein, Pseudomonas aeruginosa ; Fimbriae Proteins (147680-16-8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2009-12-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0911616107
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Article: Global nutritional profiling for mutant and chemical mode-of-action analysis in filamentous fungi.

Tanzer, Matthew M / Arst, Herbert N / Skalchunes, Amy R / Coffin, Marie / Darveaux, Blaise A / Heiniger, Ryan W / Shuster, Jeffrey R

Functional & integrative genomics

2003 Volume 3, Issue 4, Page(s) 160–170

Abstract: We describe a method for gene function discovery and chemical mode-of-action analysis via nutrient utilization using a high throughput Nutritional Profiling platform suitable for filamentous microorganisms. We have optimized the growth conditions for ... ...

Abstract	We describe a method for gene function discovery and chemical mode-of-action analysis via nutrient utilization using a high throughput Nutritional Profiling platform suitable for filamentous microorganisms. We have optimized the growth conditions for each fungal species to produce reproducible optical density growth measurements in microtiter plates. We validated the Nutritional Profiling platform using a nitrogen source utilization assay to analyze 21 Aspergillus nidulans strains with mutations in the master nitrogen regulatory gene, areA. Analysis of these data accurately reproduced expected results and provided new data to demonstrate that this platform is suitable for fine level phenotyping of filamentous fungi. Next, we analyzed the differential responses of two fungal species to a glutamine synthetase inhibitor, illustrating chemical mode-of-action analysis. Finally, a comparative phenotypic study was performed to characterize carbon catabolite repression in four fungal species using a carbon source utilization assay. The results demonstrate differentiation between two Aspergillus species and two diverse plant pathogens and provide a wealth of new data on fungal nutrient utilization. Thus, these assays can be used for gene function and chemical mode-of-action analysis at the whole organism level as well as interspecies comparisons in a variety of filamentous fungi. Additionally, because uniform distribution of growth within wells is maintained, comparisons between yeast and filamentous forms of a single organism can be performed.
MeSH term(s)	Aminobutyrates/pharmacology ; Aspergillus nidulans/genetics ; Carbon/metabolism ; Culture Media/chemistry ; Culture Media/pharmacology ; Dose-Response Relationship, Drug ; Enzyme Inhibitors/pharmacology ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Fungi/genetics ; Fungi/growth & development ; Fungi/metabolism ; Fungi/pathogenicity ; Gene Expression Profiling ; Genes, Fungal ; Glutamate-Ammonia Ligase/antagonists & inhibitors ; Kinetics ; Mutation ; Nitrogen/metabolism ; Oligonucleotide Array Sequence Analysis ; Reproducibility of Results ; Species Specificity ; Substrate Specificity
Chemical Substances	Aminobutyrates ; Culture Media ; Enzyme Inhibitors ; Fungal Proteins ; phosphinothricin (51276-47-2) ; Carbon (7440-44-0) ; Glutamate-Ammonia Ligase (EC 6.3.1.2) ; Nitrogen (N762921K75)
Language	English
Publishing date	2003-12
Publishing country	Germany
Document type	Comparative Study ; Journal Article
ZDB-ID	2014670-X
ISSN	1438-7948 ; 1438-793X
ISSN (online)	1438-7948
ISSN	1438-793X
DOI	10.1007/s10142-003-0089-3
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Article ; Online: Genetic and functional analyses of PptA, a phospho-form transferase targeting type IV pili in Neisseria gonorrhoeae.

Naessan, Cecilia L / Egge-Jacobsen, Wolfgang / Heiniger, Ryan W / Wolfgang, Matthew C / Aas, Finn Erik / Røhr, Asmund / Winther-Larsen, Hanne C / Koomey, Michael

Journal of bacteriology

2007 Volume 190, Issue 1, Page(s) 387–400

Abstract: The PilE pilin subunit protein of Neisseria gonorrhoeae undergoes unique covalent modifications with phosphoethanolamine (PE) and phosphocholine (PC). The pilin phospho-form transferase A (PptA) protein, required for these modifications, shows sequence ... ...

Abstract	The PilE pilin subunit protein of Neisseria gonorrhoeae undergoes unique covalent modifications with phosphoethanolamine (PE) and phosphocholine (PC). The pilin phospho-form transferase A (PptA) protein, required for these modifications, shows sequence relatedness with and architectural similarities to lipopolysaccharide PE transferases. Here, we used regulated expression and mutagenesis as means to better define the relationships between PptA structure and function, as well as to probe the mechanisms by which other factors impact the system. We show here that pptA expression is coupled at the level of transcription to its distal gene, murF, in a division/cell wall gene operon and that PptA can act in a dose-dependent fashion in PilE phospho-form modification. Molecular modeling and site-directed mutagenesis provided the first direct evidence that PptA is a member of the alkaline phosphatase superfamily of metalloenzymes with similar metal-binding sites and conserved structural folds. Through phylogenetic analyses and sequence alignments, these conclusions were extended to include the lipopolysaccharide PE transferases, including members of the disparate Lpt6 subfamily, and the MdoB family of phosphoglycerol transferases. Each of these enzymes thus likely acts as a phospholipid head group transferase whose catalytic mechanism involves a trans-esterification step generating a protein-phospho-form ester intermediate. Coexpression of PptA with PilE in Pseudomonas aeruginosa resulted in high levels of PE modification but was not sufficient for PC modification. This and other findings show that PptA-associated PC modification is governed by as-yet-undefined ancillary factors unique to N. gonorrhoeae.
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Fimbriae, Bacterial/drug effects ; Fimbriae, Bacterial/enzymology ; Fimbriae, Bacterial/genetics ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Immunoblotting ; Microbial Sensitivity Tests ; Mutagenesis ; Neisseria gonorrhoeae/enzymology ; Neisseria gonorrhoeae/genetics ; Plasmids ; Promoter Regions, Genetic ; Pseudomonas aeruginosa/enzymology ; Pseudomonas aeruginosa/genetics ; Recombinant Proteins/metabolism ; Transferases (Other Substituted Phosphate Groups)/genetics ; Transferases (Other Substituted Phosphate Groups)/metabolism
Chemical Substances	Anti-Bacterial Agents ; Recombinant Proteins ; PptA protein, Neisseria meningitidis (EC 2.7.8.-) ; Transferases (Other Substituted Phosphate Groups) (EC 2.7.8.-)
Language	English
Publishing date	2007-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00765-07
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Article: Sequence analysis and functional characterization of the dialkylglycine decarboxylase gene DGD1 from Mycosphaerella graminicola.

Adachi, Kiichi / Nelson, Grant H / Peoples, Keith A / DeZwaan, Todd M / Skalchunes, Amy R / Heiniger, Ryan W / Shuster, Jeffrey R / Hamer, Lisbeth / Tanzer, Matthew M

Current genetics

2003 Volume 43, Issue 5, Page(s) 358–363

Abstract: Dialkylglycine decarboxylase is a pyridoxal phosphate-dependent enzyme in the aminotransferases class III group of enzymes. The enzyme is unique in terms of catalyzing both decarboxylation and transamination. Although the enzymatic activity is present in ...

Abstract	Dialkylglycine decarboxylase is a pyridoxal phosphate-dependent enzyme in the aminotransferases class III group of enzymes. The enzyme is unique in terms of catalyzing both decarboxylation and transamination. Although the enzymatic activity is present in some bacteria and fungi, the biological role is unclear. We identified and disrupted the dialkylglycine decarboxylase-encoding gene DGD1 in the wheat blotch fungus Mycosphaerella graminicola by transposon-arrayed gene knockout. The DGD1 gene is highly similar to dialkylglycine decarboxylase from the soil bacterium Burkholderia cepacia. Phylogenetic analysis of various class III aminotransferases showed that dialkylglycine decarboxylases from bacteria and fungi are found in a distinct cluster. Functional analysis revealed that dgd1 disruption mutants display wild-type morphology and pathogenicity to wheat. The dgd1 mutants cannot utilize 2-methylalanine as a sole nitrogen source, as assessed by large-scale nutritional utilization analysis. This is the first description of a mutant phenotype of the fungal dialkylglycine decarboxylase gene.
MeSH term(s)	Amino Acid Sequence ; Aminoisobutyric Acids/metabolism ; Ascomycota/enzymology ; Ascomycota/genetics ; Blotting, Southern ; Carboxy-Lyases/genetics ; Carboxy-Lyases/metabolism ; Chromosome Mapping ; DNA Primers ; Molecular Sequence Data ; Phylogeny ; Sequence Analysis, DNA ; Transformation, Genetic
Chemical Substances	Aminoisobutyric Acids ; DNA Primers ; 2-aminoisobutyric acid (1E7ZW41IQU) ; Carboxy-Lyases (EC 4.1.1.-) ; 2,2-dialkylglycine decarboxylase (EC 4.1.1.64)
Language	English
Publishing date	2003-08
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-003-0402-7
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