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1.
Microbiologyopen ; 13(4): e1425, 2024 Aug.
Article in English | MEDLINE | ID: mdl-38987999

ABSTRACT

Pigments provide a simple means to rapidly visually ascertain the quantities or presence of specific microbes in a complex community. The selection of pigment-producing colonies that are simple to differentiate from common colony phenotypes provides a high degree of certainty for the identity of pigment-tagged strains. Successful employment of pigment production is dependent on various intrinsic factors related to proper levels of gene expression and pigment production that are not always easy to predict and vary within each microbe. We have constructed a simple transposon system that incorporates the genes for the production of deoxyviolacein, a pigment produced from intracellular reserves of the amino acid tryptophan, to randomly insert these genes throughout the genome. This tool allows the user to select from many thousands of potential sites throughout a bacterial genome for an ideal location to generate the desired amount of pigment. We have applied this system to a small selection of endophytes and other model bacteria to differentiate these strains from complex communities and confirm their presence after several weeks in natural environments. We provide two examples of applications using the pigments to trace strains following introduction into plant tissues or to produce a reporter strain for extracellular nitrogen compound sensing. We recognize that this tool could have far broader utility in other applications and microbes, and describe the methodology for use by the greater scientific community.


Subject(s)
DNA Transposable Elements , Pigments, Biological , DNA Transposable Elements/genetics , Pigments, Biological/metabolism , Mutagenesis, Insertional/methods , Genetic Vectors/genetics , Bacteria/genetics , Bacteria/metabolism , Bacteria/classification , Tryptophan/metabolism , Endophytes/genetics , Endophytes/metabolism
2.
Microbiol Spectr ; 12(1): e0247823, 2024 Jan 11.
Article in English | MEDLINE | ID: mdl-38038458

ABSTRACT

IMPORTANCE: Our results demonstrate increased extracellular ammonium release in the endophyte plant growth-promoting bacterium Gluconacetobacter diazotrophicus. Strains were constructed in a manner that leaves no antibiotic markers behind, such that these strains contain no transgenes. Levels of ammonium achieved by cultures of modified G. diazotrophicus strains reached concentrations of approximately 18 mM ammonium, while wild-type G. diazotrophicus remained much lower (below 50 µM). These findings demonstrate a strong potential for further improving the biofertilizer potential of this important microbe.


Subject(s)
Endophytes , Gluconacetobacter , Endophytes/genetics , Gene Editing , Gluconacetobacter/genetics
3.
Appl Environ Microbiol ; 88(23): e0124122, 2022 12 13.
Article in English | MEDLINE | ID: mdl-36374093

ABSTRACT

Plant growth-promoting (PGP) bacteria are important to the development of sustainable agricultural systems. PGP microbes that fix atmospheric nitrogen (diazotrophs) could minimize the application of industrially derived fertilizers and function as a biofertilizer. The bacterium Gluconacetobacter diazotrophicus is a nitrogen-fixing PGP microbe originally discovered in association with sugarcane plants, where it functions as an endophyte. It also forms endophyte associations with a range of other agriculturally relevant crop plants. G. diazotrophicus requires microaerobic conditions for diazotrophic growth. We generated a transposon library for G. diazotrophicus and cultured the library under various growth conditions and culture medium compositions to measure fitness defects associated with individual transposon inserts (transposon insertion sequencing [Tn-seq]). Using this library, we probed more than 3,200 genes and ascertained the importance of various genes for diazotrophic growth of this microaerobic endophyte. We also identified a set of essential genes. IMPORTANCE Our results demonstrate a succinct set of genes involved in diazotrophic growth for G. diazotrophicus, with a lower degree of redundancy than what is found in other model diazotrophs. The results will serve as a valuable resource for those interested in biological nitrogen fixation and will establish a baseline data set for plant free growth, which could complement future studies related to the endophyte relationship.


Subject(s)
Gluconacetobacter , Symbiosis , Gluconacetobacter/genetics , Nitrogen Fixation/genetics , Nitrogen
4.
Arch Virol ; 167(2): 631-634, 2022 Feb.
Article in English | MEDLINE | ID: mdl-35028739

ABSTRACT

The complete genome sequences of two isolates of spiraea yellow leafspot virus (SYLSV) were determined. Spiraea (Spiraea x bumalda) 'Anthony Waterer' plants showing virus-like symptoms including yellow spotting and leaf deformation were used for sequencing. The viral genome of SYLSV-MN (Minnesota) and SYLSV-MD (Maryland) is 8,017bp in length. The sequences share 95% identity at the nucleotide level. Both isolates have the same genome organization containing three open reading frames (ORFs), with ORF3 being the largest, encoding a putative polyprotein of 232 kDa with conserved domains including a zinc finger, pepsin-like aspartate protease, reverse transcriptase (RT), and RNase H. Pairwise comparisons between members of the genus Badnavirus showed that gooseberry vein banding associated virus GB1 (HQ852248) and rubus yellow net virus isolate Baumforth's Seedling A (KM078034) were the closest related virus sequences to SYLSV, sharing 73% identity at the nucleotide level. Bacilliform virions with dimensions of 150 nm × 30 nm were observed in virus preparations from symptomatic, but not asymptomatic, plants.


Subject(s)
Badnavirus , Spiraea , Badnavirus/genetics , Genome, Viral , Open Reading Frames , Phylogeny , Plant Diseases
5.
J Gen Virol ; 101(10): 1025-1026, 2020 10.
Article in English | MEDLINE | ID: mdl-32940596

ABSTRACT

Caulimoviridae is a family of non-enveloped reverse-transcribing plant viruses with non-covalently closed circular dsDNA genomes of 7.1-9.8 kbp in the order Ortervirales. They infect a wide range of monocots and dicots. Some viruses cause economically important diseases of tropical and subtropical crops. Transmission occurs through insect vectors (aphids, mealybugs, leafhoppers, lace bugs) and grafting. Activation of infectious endogenous viral elements occurs in Musa balbisiana, Petunia hybrida and Nicotiana edwardsonii. However, most endogenous caulimovirids are not infectious. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the family Caulimoviridae, which is available at ictv.global/report/caulimoviridae.


Subject(s)
Caulimoviridae , Caulimoviridae/classification , Caulimoviridae/physiology , Caulimoviridae/ultrastructure , Genome, Viral , Plants/virology , Virus Replication
6.
Plant Biotechnol J ; 17(1): 132-140, 2019 01.
Article in English | MEDLINE | ID: mdl-29797460

ABSTRACT

The tomato PROCERA gene encodes a DELLA protein, and loss-of-function mutations derepress growth. We used CRISPR/Cas9 and a single guide RNAs (sgRNA) to target mutations to the PROCERA DELLA domain, and recovered several loss-of-function mutations and a dominant dwarf mutation that carries a deletion of one amino acid in the DELLA domain. This is the first report of a dominant dwarf PROCERA allele. This allele retains partial responsiveness to exogenously applied gibberellin. Heterozygotes show an intermediate phenotype at the seedling stage, but adult heterozygotes are as dwarfed as homozygotes.


Subject(s)
CRISPR-Associated Protein 9 , CRISPR-Cas Systems , Gene Editing , Gibberellins/metabolism , Plant Growth Regulators/metabolism , Solanum lycopersicum/genetics , Alleles , Gene Editing/methods , Genes, Plant , Heterozygote , Homozygote , Solanum lycopersicum/growth & development , Peptides , Plant Proteins/genetics , Plant Proteins/metabolism
9.
Plant Cell ; 29(12): 3186-3197, 2017 12.
Article in English | MEDLINE | ID: mdl-29150547

ABSTRACT

Plants employ stomatal closure and reduced growth to avoid water deficiency damage. Reduced levels of the growth-promoting hormone gibberellin (GA) lead to increased tolerance to water deficit, but the underlying mechanism is unknown. Here, we show that the tomato (Solanum lycopersicum) DELLA protein PROCERA (PRO), a negative regulator of GA signaling, acts in guard cells to promote stomatal closure and reduce water loss in response to water deficiency by increasing abscisic acid (ABA) sensitivity. The loss-of-function pro mutant exhibited increased stomatal conductance and rapid wilting under water deficit stress. Transgenic tomato overexpressing constitutively active stable DELLA proteins (S-della) displayed the opposite phenotype. The effects of S-della on stomatal aperture and water loss were strongly suppressed in the ABA-deficient mutant sitiens, indicating that these effects of S-della are ABA dependent. While DELLA had no effect on ABA levels, guard cell ABA responsiveness was increased in S-della and reduced in pro plants compared with the wild type. Expressing S-della under the control of a guard-cell-specific promoter was sufficient to increase stomatal sensitivity to ABA and to reduce water loss under water deficit stress but had no effect on leaf size. This result indicates that DELLA promotes stomatal closure independently of its effect on growth.


Subject(s)
Plant Proteins/metabolism , Plant Stomata/cytology , Plant Stomata/physiology , Solanum lycopersicum/metabolism , Solanum lycopersicum/physiology , Abscisic Acid/pharmacology , Arabidopsis Proteins/metabolism , Gene Expression Regulation, Plant/drug effects , Solanum lycopersicum/genetics , Models, Biological , Mutation/genetics , Plant Transpiration/physiology , Plants, Genetically Modified , Stress, Physiological , Water
10.
Virus Res ; 241: 62-67, 2017 09 15.
Article in English | MEDLINE | ID: mdl-28559100

ABSTRACT

A disease of Rudbeckia hirta (Black-eyed Susan), characterized by severe flower deformation, was observed in Minnesota during 2010-2016. A previously undescribed virus species, named Rudbeckia flower distortion virus (RuFDV, family Caulimoviridae, genus unassigned), was determined to be the causal agent of the disease. Symptoms induced by RuFDV infection resemble those characteristic of phytoplasma-induced diseases, but no phytoplasmas were detected in RuFDV-infected R. hirta. The virus, and the disease were transmitted readily by mechanical inoculation and by the aphid Myzus persicae, but only to R. hirta. Virions of RuFDV are icosahedral, 42-45nm in diameter, and contain a circular 8222bp dsDNA genome containing seven open reading frames (ORFs). The ORFs 2-6 have 28-52% amino acid sequence identity to the movement protein (MP), coat protein (CP), aspartic protease (AP), reverse transcriptase (RT) and RNase H, and translational transactivator (TA) domains of known caulimoviruses. The two remaining ORFs (1 and 7) have no significant amino acid sequence similarity to known viruses. Although the RuFDV ORF 6 is significantly truncated relative to those of other known caulimoviruses, neither this nor the concomitant absence of characteristic virus-encoded cytoplasmic inclusion bodies appears to adversely affect aphid transmission of this virus. Phylogenetic analysis based on the sequence of the RT region revealed no close relationship to known members of the family Caulimoviridae. Based on sequence similarity, genome organization and phylogenetic relatedness, RuFDV appears to be distinct from any currently recognized taxonomic grouping in the family Caulimoviridae.


Subject(s)
Caulimoviridae/classification , Caulimoviridae/genetics , Flowers/virology , Plant Diseases/virology , Rudbeckia/virology , Amino Acid Sequence , Animals , Aphids/virology , Aspartic Acid Proteases/genetics , Capsid Proteins/genetics , Insect Vectors/virology , Plant Viral Movement Proteins/genetics , RNA-Directed DNA Polymerase/genetics , Ribonuclease H/genetics , Sequence Homology, Amino Acid
11.
Nat Chem Biol ; 13(5): 479-485, 2017 05.
Article in English | MEDLINE | ID: mdl-28244988

ABSTRACT

Plant development requires coordination among complex signaling networks to enhance the plant's adaptation to changing environments. DELLAs, transcription regulators originally identified as repressors of phytohormone gibberellin signaling, play a central role in integrating multiple signaling activities via direct protein interactions with key transcription factors. Here, we found that DELLA is mono-O-fucosylated by the novel O-fucosyltransferase SPINDLY (SPY) in Arabidopsis thaliana. O-fucosylation activates DELLA by promoting its interaction with key regulators in brassinosteroid- and light-signaling pathways, including BRASSINAZOLE-RESISTANT1 (BZR1), PHYTOCHROME-INTERACTING-FACTOR3 (PIF3) and PIF4. Moreover, spy mutants displayed elevated responses to gibberellin and brassinosteroid, and increased expression of common target genes of DELLAs, BZR1 and PIFs. Our study revealed that SPY-dependent protein O-fucosylation plays a key role in regulating plant development. This finding may have broader importance because SPY orthologs are conserved in prokaryotes and eukaryotes, thus suggesting that intracellular O-fucosylation may regulate a wide range of biological processes in diverse organisms.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Fucosyltransferases/metabolism , Repressor Proteins/metabolism , Arabidopsis/enzymology , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Fucosyltransferases/genetics , Repressor Proteins/genetics
12.
Plant Physiol ; 173(2): 1453-1462, 2017 02.
Article in English | MEDLINE | ID: mdl-27999086

ABSTRACT

The plant hormone indole-3-acetic acid (IAA or auxin) mediates the elongation growth of shoot tissues by promoting cell expansion. According to the acid growth theory proposed in the 1970s, auxin activates plasma membrane H+-ATPases (PM H+-ATPases) to facilitate cell expansion by both loosening the cell wall through acidification and promoting solute uptake. Mechanistically, however, this process is poorly understood. Recent findings in Arabidopsis (Arabidopsis thaliana) have demonstrated that auxin-induced SMALL AUXIN UP RNA (SAUR) genes promote elongation growth and play a key role in PM H+-ATPase activation by inhibiting PP2C.D family protein phosphatases. Here, we extend these findings by demonstrating that SAUR proteins also inhibit tomato PP2C.D family phosphatases and that AtSAUR19 overexpression in tomato (Solanum lycopersicum) confers the same suite of phenotypes as previously reported for Arabidopsis. Furthermore, we employ a custom image-based method for measuring hypocotyl segment elongation with high resolution and a method for measuring cell wall mechanical properties, to add mechanistic details to the emerging description of auxin-mediated cell expansion. We find that constitutive expression of GFP-AtSAUR19 bypasses the normal requirement of auxin for elongation growth by increasing the mechanical extensibility of excised hypocotyl segments. In contrast, hypocotyl segments overexpressing a PP2C.D phosphatase are specifically impaired in auxin-mediated elongation. The time courses of auxin-induced SAUR expression and auxin-dependent elongation growth were closely correlated. These findings indicate that induction of SAUR expression is sufficient to elicit auxin-mediated expansion growth by activating PM H+-ATPases to facilitate apoplast acidification and mechanical wall loosening.


Subject(s)
Arabidopsis Proteins/genetics , Hypocotyl/growth & development , Indoleacetic Acids/metabolism , Solanum lycopersicum/growth & development , Arabidopsis Proteins/metabolism , Gene Expression Regulation, Plant , Green Fluorescent Proteins/genetics , Green Fluorescent Proteins/metabolism , Hypocotyl/genetics , Hypocotyl/metabolism , Solanum lycopersicum/genetics , Plants, Genetically Modified , Protein Phosphatase 2C/genetics , Protein Phosphatase 2C/metabolism , Proton-Translocating ATPases/metabolism
14.
Genes Dev ; 30(2): 164-76, 2016 Jan 15.
Article in English | MEDLINE | ID: mdl-26773002

ABSTRACT

The DELLA family of transcription regulators functions as master growth repressors in plants by inhibiting phytohormone gibberellin (GA) signaling in response to developmental and environmental cues. DELLAs also play a central role in mediating cross-talk between GA and other signaling pathways via antagonistic direct interactions with key transcription factors. However, how these crucial protein-protein interactions can be dynamically regulated during plant development remains unclear. Here, we show that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET AGENT (SEC) in Arabidopsis. O-GlcNAcylation of the DELLA protein REPRESSOR OF ga1-3 (RGA) inhibits RGA binding to four of its interactors-PHYTOCHROME-INTERACTING FACTOR3 (PIF3), PIF4, JASMONATE-ZIM DOMAIN1, and BRASSINAZOLE-RESISTANT1 (BZR1)-that are key regulators in light, jasmonate, and brassinosteroid signaling pathways, respectively. Consistent with this, the sec-null mutant displayed reduced responses to GA and brassinosteroid and showed decreased expression of several common target genes of DELLAs, BZR1, and PIFs. Our results reveal a direct role of OGT in repressing DELLA activity and indicate that O-GlcNAcylation of DELLAs provides a fine-tuning mechanism in coordinating multiple signaling activities during plant development.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/physiology , Gene Expression Regulation, Plant/genetics , N-Acetylglucosaminyltransferases/metabolism , Signal Transduction/physiology , Acylation , Arabidopsis/growth & development , Arabidopsis Proteins/genetics , Gibberellins/metabolism , Mutation , N-Acetylglucosaminyltransferases/genetics , Protein Binding
15.
Essays Biochem ; 58: 49-60, 2015.
Article in English | MEDLINE | ID: mdl-26374886

ABSTRACT

Gibberellins (GAs) are phytohormones that regulate growth and development. DELLA proteins repress GA responses. GA binding to its receptor triggers a series of events that culminate in the destruction of DELLA proteins by the 26S proteasome, which removes the repression of GA signalling. DELLA proteins are transcription co-activators that induce the expression of genes which encode products that inhibit GA responses. In addition to repressing GA responses, DELLA proteins influence the activity of other signalling pathways and serve as a central hub from which other pathways influence GA signalling. In this role, DELLA proteins bind to and inhibit proteins, including transcription factors that act in the signalling pathways of other hormones and light. The binding of these proteins to DELLA proteins also inhibits DELLA activity. GA signalling is subject to homoeostatic regulation through GA-induced repression of GA biosynthesis gene expression, and increased production of the GA receptor and enzymes that catabolize bioactive GAs. This review also discusses the nature of mutant DELLA alleles that are used to produce high-yielding 'Green Revolution' cereal varieties, and highlights important gaps in our knowledge of GA signalling.


Subject(s)
Gibberellins/metabolism , Plant Growth Regulators/metabolism , Signal Transduction , Homeostasis , Plant Proteins/physiology , Trans-Activators/physiology
16.
Plant Cell ; 27(6): 1579-94, 2015 Jun.
Article in English | MEDLINE | ID: mdl-26036254

ABSTRACT

Gibberellin (GA) regulates plant development primarily by triggering the degradation/deactivation of the DELLA proteins. However, it remains unclear whether all GA responses are regulated by DELLAs. Tomato (Solanum lycopersicum) has a single DELLA gene named PROCERA (PRO), and its recessive pro allele exhibits constitutive GA activity but retains responsiveness to external GA. In the loss-of-function mutant pro(ΔGRAS), all examined GA developmental responses were considerably enhanced relative to pro and a defect in seed desiccation tolerance was uncovered. As pro, but not pro(ΔGRAS), elongation was promoted by GA treatment, pro may retain residual DELLA activity. In agreement with homeostatic feedback regulation of the GA biosynthetic pathway, we found that GA20oxidase1 expression was suppressed in pro(ΔGRAS) and was not affected by exogenous GA3. In contrast, expression of GA2oxidase4 was not affected by the elevated GA signaling in pro(ΔGRAS) but was strongly induced by exogenous GA3. Since a similar response was found in Arabidopsis thaliana plants with impaired activity of all five DELLA genes, we suggest that homeostatic GA responses are regulated by both DELLA-dependent and -independent pathways. Transcriptome analysis of GA-treated pro(ΔGRAS) leaves suggests that 5% of all GA-regulated genes in tomato are DELLA independent.


Subject(s)
Gibberellins/physiology , Plant Growth Regulators/physiology , Plant Proteins/physiology , Solanum lycopersicum/physiology , Abscisic Acid/physiology , Feedback, Physiological , Genes, Plant/physiology , Solanum lycopersicum/genetics , Mutation , Plant Growth Regulators/genetics , Plant Proteins/genetics , Seeds/growth & development , Seeds/physiology , Transcriptome
17.
J Bacteriol ; 197(2): 354-61, 2015 Jan.
Article in English | MEDLINE | ID: mdl-25384478

ABSTRACT

The posttranslational addition of a single O-linked ß-N-acetylglucosamine (O-GlcNAc) to serine or threonine residues regulates numerous metazoan cellular processes. The enzyme responsible for this modification, O-GlcNAc transferase (OGT), is conserved among a wide variety of organisms and is critical for the viability of many eukaryotes. Although OGTs with domain structures similar to those of eukaryotic OGTs are predicted for many bacterial species, the cellular roles of these OGTs are unknown. We have identified a putative OGT in the cyanobacterium Synechococcus elongatus PCC 7942 that shows active-site homology and similar domain structure to eukaryotic OGTs. An OGT deletion mutant was created and found to exhibit several phenotypes. Without agitation, mutant cells aggregate and settle out of the medium. The mutant cells have higher free inorganic phosphate levels, wider thylakoid lumen, and differential accumulation of electron-dense inclusion bodies. These phenotypes are rescued by reintroduction of the wild-type OGT but are not fully rescued by OGTs with single amino acid substitutions corresponding to mutations that reduce eukaryotic OGT activity. S. elongatus OGT purified from Escherichia coli hydrolyzed the sugar donor, UDP-GlcNAc, while the mutant OGTs that did not fully rescue the deletion mutant phenotypes had reduced or no activity. These results suggest that bacterial eukaryote-like OGTs, like their eukaryotic counterparts, influence multiple processes.


Subject(s)
N-Acetylglucosaminyltransferases/metabolism , Synechococcus/enzymology , Synechococcus/metabolism , N-Acetylglucosaminyltransferases/genetics , Synechococcus/genetics
19.
Virology ; 442(2): 122-31, 2013 Aug 01.
Article in English | MEDLINE | ID: mdl-23639873

ABSTRACT

O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.


Subject(s)
Acetylglucosamine/metabolism , Capsid Proteins/metabolism , Plum Pox Virus/pathogenicity , Protein Processing, Post-Translational , Arabidopsis/virology , Capsid Proteins/chemistry , DNA Mutational Analysis , Plant Diseases/virology , Plum Pox Virus/chemistry , Prunus/virology , Nicotiana/virology
20.
Plant Physiol ; 161(1): 455-64, 2013 Jan.
Article in English | MEDLINE | ID: mdl-23144189

ABSTRACT

Many plant proteins are modified with N-linked oligosaccharides at asparagine-X-serine/threonine sites during transit through the endoplasmic reticulum and the Golgi. We have identified a number of Arabidopsis (Arabidopsis thaliana) proteins with modifications consisting of an N-linked N-acetyl-D-glucosamine monosaccharide (N-GlcNAc). Electron transfer dissociation mass spectrometry analysis of peptides bearing this modification mapped the modification to asparagine-X-serine/threonine sites on proteins that are predicted to transit through the endoplasmic reticulum and Golgi. A mass labeling method was developed and used to study N-GlcNAc modification of two thioglucoside glucohydrolases (myrosinases), TGG1 and TGG2 (for thioglucoside glucohydrolase). These myrosinases are also modified with high-mannose (Man)-type glycans. We found that N-GlcNAc and high-Man-type glycans can occur at the same site. It has been hypothesized that N-GlcNAc modifications are generated when endo-ß-N-acetylglucosaminidase (ENGase) cleaves N-linked glycans. We examined the effects of mutations affecting the two known Arabidopsis ENGases on N-GlcNAc modification of myrosinase and found that modification of TGG2 was greatly reduced in one of the single mutants and absent in the double mutant. Surprisingly, N-GlcNAc modification of TGG1 was not affected in any of the mutants. These data support the hypothesis that ENGases hydrolyze high-Man glycans to produce some of the N-GlcNAc modifications but also suggest that some N-GlcNAc modifications are generated by another mechanism. Since N-GlcNAc modification was detected at only one site on each myrosinase, the production of the N-GlcNAc modification may be regulated.


Subject(s)
Acetylglucosamine/metabolism , Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Glycoside Hydrolases/metabolism , Amino Acid Sequence , Arabidopsis/enzymology , Arabidopsis Proteins/genetics , Asparagine/metabolism , Chromatography, Affinity/methods , Cytosol/metabolism , Endoplasmic Reticulum/metabolism , Enzyme Activation , Glycoside Hydrolases/genetics , Glycosylation , Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase/metabolism , Molecular Conformation , Polysaccharides/metabolism , Protein Folding , Recombinant Proteins/metabolism , Serine/metabolism , Threonine/metabolism
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