Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato).

Pautot, Véronique; Holzer, Frances M.; Reisch, Bruce I.; Walling, Linda L.

doi:10.1073/pnas.90.21.9906

Cited by 114 publications

(123 citation statements)

References 48 publications

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“…However, LapA RNAs, proteins, and activities accumulate locally and systemically in leaves after wounding, Pseudomonas syringae pv. tomato and Phytophthora parasitica infection, and caterpillar feeding (Pautot et al, 1993(Pautot et al, , 2001Gu et al, 1996b;Chao et al, 1999;Jwa and Walling, 2001). The activation of LapA gene expression by jasmonic acid (JA), abscisic acid, the phytotoxin coronatine (a JA mimic), and suppression of LapA by salicylic acid is consistent with the regulation of the tomato LapA genes by the wound octadecanoid pathway (Chao et al, 1999).…”

mentioning

confidence: 58%

“…A, Four GST-LapN fusion genes containing domains A, B, D, and F were constructed and overexpressed in E. coli. Black bars, LapA1-coding regions in the 1.9-kb full-length LapA1 cDNA clone pBLapA1 (Gu et al, 1996a), the partial LapA1 cDNA clone pDR57 corresponding to LapA1 nucleotides 325 to 1,843 (Pautot et al, 1993), and the GSTLapA fusion constructs. The glutathione-S-transferase (GST)-LAP-A fusion proteins contained the following amino acid residues: A (residues 123-194), B (residues 195-233), D (residues 290-424), and F (residues 534-571).…”

Section: Lap-n and Lap-a Protein Accumulation In Vegetative And Repromentioning

confidence: 99%

“…Eleven plant LAPs were aligned to elucidate their relatedness to the tomato LAP-N ( Fig. 6; Bartling and Weiler, 1992;Hildmann et al, 1992;Pautot et al, 1993;Milligan and Gasser, 1995;Gu et al, 1996a;Valjakka et al, 1999). The Conserved Domain Database (National Center for Biotechnology Information) identified two conserved Pfam domains (Fig.…”

Section: Rnas and Proteinsmentioning

confidence: 99%

“…A similar pattern of expression was noted for the potato LAP (Hildmann et al, 1992;Dammann et al, 1997), which shared the LAP-A signature residues. Because LAP-A proteins are detected in leaves after wounding and infection (Pautot et al, 1993;Gu et al, 1996b) and in reproductive organs, LAP-A may have a more specialized role than LAP-N. It is possible that the LAP-A proteins have a role in protecting male and female reproduction organs from insect attack or pathogen infection (Milligan and Gasser, 1995;Pautot et al, 2001).…”

Section: Lap-n and Lap-a1 Enzyme Activity On Amino Acyl-␤ -Nap Subsmentioning

confidence: 99%

“…U50151; Gu et al, 1996a). pDR57 is a partial LapA1 cDNA clone corresponding to nucleotides 325 to 1,843 (Pautot et al, 1993). pDR57 was digested with PstI and DNA fragments were end filled with T4 DNA polymerase and subcloned into SmaI-digested pGEX-3X to give rise to pGLAPA-A (nucleotides 390-600; domain A) and pGLAPA-B 9 (nucleotides 601-954).…”

Section: Isolation Of Lap-a Domain-specific Antibodiesmentioning

confidence: 99%

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Isolation and Characterization of the Neutral Leucine Aminopeptidase (LapN) of Tomato

Park

Walling

2003

Plant Physiology

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Tomatoes (Lycopersicon esculentum) express two forms of leucine aminopeptidase (LAP-A and LAP-N) and two LAP-like proteins. The relatedness of LAP-N and LAP-A was determined using affinity-purified antibodies to four LAP-A protein domains. Antibodies to epitopes in the most N-terminal region were able to discriminate between LAP-A and LAP-N, whereas antibodies recognizing central and COOH-terminal regions recognized both LAP polypeptides. Two-dimensional immunoblots showed that LAP-N and the LAP-like proteins were detected in all vegetative (leaves, stems, roots, and cotyledons) and reproductive (pistils, sepals, petals, stamens, and floral buds) organs examined, whereas LAP-A exhibited a distinct expression program. LapN was a single-copy gene encoding a rare-class transcript. A full-length LapN cDNA clone was isolated, and the deduced sequence had 77% peptide sequence identity with the wound-induced LAP-A. Leucyl aminopeptidases (LAPs; EC 3.4.11.1) are members of the M17 family of peptidases (Barrett et al., 1998). LAPs are ubiquitous being found in animals, plants, and prokaryotic cells. These hexameric metallopeptidases catalyze the release of the N-terminal residues from protein, peptide, fluorometric, and chromogenic substrates. The best characterized LAPs are from Bos taurus, Escherichia coli and tomato (Lycopersicon esculentum). X-ray crystal structures of the bovine and E. coli LAPs have provided insight into the LAP catalytic mechanism (Kim and Lipscomb, 1994;Sträter and Lipscomb, 1995;Sträter et al., 1999a). The roles of selected residues of the E. coli and tomato LAPs in chromogenic or peptide substrate catalysis, respectively, have been tested by site-directed mutagenesis (Sträter et al., 1999b;Gu and Walling, 2002).In most plants, three classes of LAP-related polypeptides are detected using a tomato LAP antiserum, including the 66-and 77-kD LAP-like proteins and the 55-kD neutral LAP (LAP-N; Chao et al., 2000). Only in a subset of the Solanaceae is a second 55-kD LAP species (LAP-A) detected (Hildmann et al., 1992;Gu et al., 1996b;Chao et al., 2000). In tomato, LAP-A protomers have an acidic pI and are encoded by two genes (LapA1 and LapA2), which are expressed during floral and fruit development. The LapA genes are not expressed in foliage from healthy plants (Chao et al., 1999). However, LapA RNAs, proteins, and activities accumulate locally and systemically in leaves after wounding, Pseudomonas syringae pv. tomato and Phytophthora parasitica infection, and caterpillar feeding (Pautot et al., 1993(Pautot et al., , 2001Gu et al., 1996b;Chao et al., 1999;Jwa and Walling, 2001). The activation of LapA gene expression by jasmonic acid (JA), abscisic acid, the phytotoxin coronatine (a JA mimic), and suppression of LapA by salicylic acid is consistent with the regulation of the tomato LapA genes by the wound octadecanoid pathway (Chao et al., 1999). LapA genes also respond to signals generated during water deficit and salinity stress (Chao et al., 1999). The potato (Solanum tuberosum) Lap RNAs also ac...

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mentioning

confidence: 58%

Section: Lap-n and Lap-a Protein Accumulation In Vegetative And Repromentioning

confidence: 99%

Section: Rnas and Proteinsmentioning

confidence: 99%

Section: Lap-n and Lap-a1 Enzyme Activity On Amino Acyl-␤ -Nap Subsmentioning

confidence: 99%

Section: Isolation Of Lap-a Domain-specific Antibodiesmentioning

confidence: 99%

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Isolation and Characterization of the Neutral Leucine Aminopeptidase (LapN) of Tomato

Park

Walling

2003

Plant Physiology

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Systemin – a polypeptide defense signal in plants

1996

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Insect and pathogen attacks activate plant defense genes within minutes in nearby cells, and within hours in leaves far distant from the sites of the predator attacks. A search for signal molecules involved in both the localized and distal signalling has resulted in the identification of an 18-amino-acid polypeptide, called systemin, that activates defense genes in leaves of tomato plants when supplied at levels as low as fmols/plant. Several lines of evidence support a role for systemin as a wound hormone. As with animal polypeptide hormones, systemin is derived from a larger precursor protein, called prosystemin, by limited proteolysis. Systemin has been shown by autoradiography to be phloemmobile and, by antisense technology, to be an essential component of the wound-inducible, systemic signal transduction system leading to the transcriptional activation of the defensive genes. A search for the receptor of systemin has led to the identification in plant plasma membranes of a systemin-binding protein. However, this protein has properties not of a receptor, but of a furin-like proteinase that cleaves systemin into smaller polypeptides. Systemin and its precursor prosystemin provide prototypes for the emerging possibilities that polypeptide hormones may have broad roles in signalling environmental stress responses, and in regulating plant growth and development as well.

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Can nanotechnology deliver the promised benefits without negatively impacting soil microbial life?

Dimkpa

2014

J. Basic Microbiol.

119

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Nanotechnology exploits the enhanced reactivity of materials at the atomic scale to improve various applications for humankind. In agriculture, potential nanotechnology applications include crop protection and fertilization. However, such benefits could come with risks for the environment: non-target plants, plant-beneficial soil microbes and other life forms could be impacted if nanoparticles (nanomaterials) contaminate the environment. This review evaluates the impact of the major metallic nanoparticles (Ag, ZnO, CuO, CeO2 , TiO2 , and FeO-based nanoparticles) on soil microbes involved in agricultural processes. The current literature indicate that in addition to population and organismal-scale effects on microbes, other subtle impacts of nanoparticles are seen in the nitrogen cycle, soil enzyme activities, and processes involved in iron metabolism, phytohormone, and antibiotic production. These effects are negative or positive, the outcome being dependent on specific nanoparticles. Collectively, published results suggest that nanotechnology portends considerable, many negative, implications for soil microbes and, thus, agricultural processes that are microbially driven. Nonetheless, the potential of plant and soil microbial processes to mitigate the bioreactivity of nanoparticles also are observed. Whereas the roots of most terrestrial plants are associated with microbes, studies of nanoparticle interactions with plants and microbes are generally conducted separately. The few studies in actual microbe-plant systems found effects of nanoparticles on the functioning of arbuscular mycorrhizal fungi, nitrogen fixation, as well as on the production of microbial siderophores in the plant rhizosphere. It is suggested that a better understanding of the agro-ecological ramifications of nanoparticles would require more in-depth interactive studies in combined plant-microbe-nanoparticle systems.

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Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato).

Cited by 114 publications

References 48 publications

Isolation and Characterization of the Neutral Leucine Aminopeptidase (LapN) of Tomato

Isolation and Characterization of the Neutral Leucine Aminopeptidase (LapN) of Tomato

Systemin – a polypeptide defense signal in plants

Can nanotechnology deliver the promised benefits without negatively impacting soil microbial life?

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