2 edition of Analysis of the function and secretion of the nodulation signalling protein, NodO. found in the catalog.
Analysis of the function and secretion of the nodulation signalling protein, NodO.
John Mark Sutton
Thesis (Ph.D.), University of East Anglia, School of Biological Sciences, 1994.
NodO is a secreted repeat-containing protein that forms pores in the membrane of legume plants and assists in the perception of Nod factors [19, 20, 21]. Entry into plant cells by SP7 could be mediated by the ability of the repeats to integrate in the plant plasma by: In the Rhizobium-legume symbiosis, compatible bacteria and host plants interact through an exchange of signals: Host compounds promote the expression of bacterial biosynthetic nod (nodulation) genes leading to the production of a lipochito-oligosaccharide signal, the Nod factor (NF). The particular array of nod genes carried by a given species of Rhizobium determines the NF structure Cited by:
Perception of the calcium oscillations is a function of a calcium- and calmodulin-dependent protein kinase, and this activates nodulation gene expression via two GRAS domain transcriptional. The peribacteroid membrane (PBM) forms the structural and functional interface between the legume plant and the rhizobia. The model legume Lotus japonicus was chosen to study the proteins present at the PBM by proteome analysis. PBM was purified from root nodules by an aqueous polymer two-phase system. Extracted proteins were subjected to a global trypsin by:
Perception of the calcium oscillations is a function of a calcium- and calmodulin-dependent protein kinase, and this activates nodulation gene expression via two GRAS domain transcriptional regulators, Nodulation Signaling Pathway1 (NSP1) and NSP2, and an ERF transcription factor required for by: Nodulation and host-specific recognition of legumes such as peas and Vicia spp. are encoded by the nodulation (nod) genes of Rhizobium leguminosarum biovar viciae. One of these genes, nodO, has been shown to encode an exported protein that contains a multiple tandem repeat of a nine amino acid domain.
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Abstract. The secreted nodulation-signaling protein NodO was purified from the supernatant of cultures of Rhizobium leguminosarum biovar viciae. The native protein has a M(r) of approximat, suggesting that it exists as a dimer since the DNA sequence predicts a M(r) of 30, Pure NodO protein had no protease, pectinase, Cited by: Analysis of the function and secretion of the nodulation signalling protein, NodO.
(Thesis) Sutton JM. Publisher: University of Analysis of the function and secretion of the nodulation signalling protein Anglia  Metadata Source: The British Library Type: Thesis.
Abstract. Highlight Terms No biological terms identified. Secretion of the NodO protein is dependent on a C-terminal signal of about 24 residues (Sutton et al., ), typical of proteins secreted via a Type I secretion system.
In this work we decribe the genes (prsDE) that encode the NodO exporter and we have identified other proteins secreted via this : C.
Finnie, A. Zorreguieta, J. Downie. Abstract. On the symbiotic plasmid pRL1JI from Rhizobium leguminosarum biovar viciae thirteen nodulation genes have been identified in five operons (nodD nodABCIJ nodFEL nodMNT and nodO). The products of most of these genes (nodABCFELMN) are involved in the biosynthesis of lipo-oligosaccharide nodulation factors, while the nodD gene product is involved in the regulation of the Cited by: 1.
In addition to Nod factors, secreted proteins can contribute to nodulation ability. NodO is a protein secreted via a Type I secretion system (PrsDE) by some rhizobia and heterologous expression of nodO could extend the host range of some rhizobial strains [5, 6].Cited by: This comparison also showed that the secreted protein is not the product of N-terminal processing of a larger precursor.
A conventional N-terminal signal sequence was not detected in the NodO protein. The NodO protein has significant homology with a part (residues to ) of the hemolysin protein (HlyA) of Escherichia by: Sutton, J., Peart, J., Dean, G., and Downie, J. Analysis of the C-terminal secretion signal of the Rhizobium leguminosarum nodulation protein NodO; a potential system for the secretion of heterologous proteins during nodule invasion.
Mol. Plant Microbe Interact. 9, – doi: /MPMICited by: 6. Analysis of the role of the signal peptide domain in GmRIC1 and GmNIC1 activity As the signal peptide has been shown to control Gm RIC1 secretion (Lim et al., ), experiments were conducted to determine whether the Gm NIC1 signal peptide was functionally interchangeable with Gm by: Nod factor (Spaink et al.
) and NodO is a secreted protein that forms cation-selective pores in membranes (Sutton et al. ) and, therefore, has the potential to catalyze calciu m or. Signal peptide peptidases play an important role in the removal of remnant signal peptides in the cell membrane, a critical step for extracellular protein production.
Although these proteins are likely a central component for extracellular protein production, there has been a lack of research on whether protein secretion could be enhanced via overexpression of signal peptide by: These proteins are secreted by a mechanism that does not involve an N-terminal signal peptide.
The NodO protein is present in the growth medium of Rhizobium bacteria induced for nod gene. The prsDE genes encode a type I protein secretion system required for the secretion of the nodulation protein NodO and at least three other proteins from Rhizobium leguminosarum bv.
viciae. At least one of these proteins was predicted to be a glycanase involved in processing of bacterial exopolysaccharide (EPS).Cited by: Proteins encoded by the rhizobial nodulation genes (nod, nol, and noe genes) are involved in the synthesis and secretion of Nod factors.
The expression of these genes is activated when the bacteria perceive specific molecules, in general flavonoids that are secreted by the plant root (Zuanazzi et al., ).Cited by: Comparative and functional analysis of NODULATION SIGNALING PATHWAY 1 (NSP1) and NSP2 in rice and Medicago Wei Liu Thesis submitted in fulfilment of the requirements for the degree of doctor at Wageningen University by the authority of the Rector Magnificus M.J.
Kropff, in. Sutton JM, Peart J, Dean G, Downie JA () Analysis of the C-terminal secretion signal of the Rhizobium leguminosarum nodulation protein NodO; a potential system for the secretion of heterologous proteins during nodule : Maged M. Saad, William J. Broughton, William J.
Deakin. In addition to Nod factors, secreted proteins can contribute to nodulation ability. NodO is a protein secreted via a Type I secretion system (PrsDE) by some rhizobia and heterologous expression of nodO could extend the host range of some rhizobial strains [5,6].Cited by: T1SS are a class of ATP-binding cassette transporters that recognize substrates with a carboxy-terminal, noncleavable signal sequence.
Through analysis of in-frame deletions, a 24 amino acid carboxy-terminal secretion signal was identified in NodO (Sutton et al., ).Cited by: These auxin changes may be caused by local inhibition of polar auxin transporters by accumulation of flavonoids.
Auxin is required for lateral root development and a parallel role for auxin in nodule development appears likely. Even in spontaneous nodulation gain-of-function mutants, the nodules formed are discrete.
Later, an LRR-RLK KLAVIER (KLV), which is highly homologous to the Arabidopsis RPK2 receptor kinase, was found to negatively regulate nodulation in L. japonicus. Double mutant analysis indicates that HAR and KLV act in the same signaling pathway. Biochemical analyses reveal a direct interaction between these two RLKs.
Therefore, nodZ represents a unique nodulation gene that is not under the control of NodD and yet is essential for the synthesis of an active nodulation signal. Full text Get a printable copy (PDF file) of the complete article (M), or click on a page image below to browse page by page.
One such mutant (A) also appeared to be defective in secretion of the R. leguminosarum nodulation protein NodO. Genetic analysis showed that the defect in A was caused by the Tn5 insertion.
However the DNA sequence adjacent to the site of Tn5 insertion had significant homology to the Escherichia coli polA gene, which encodes DNA polymerase by: 6. This secretion signal allows a flexible strategy for the production and secretion of recombinant proteins in numerous hosts, and to conveniently and rapidly study protein expression.
Introduction With innovative genomics technology, genes are being discovered faster than their functions can be by: The focus of research on signalling in Rhizobium–legume interactions has moved from understanding the structure and synthesis of rhizobially made Nod factors, towards an analysis of how they function in -factor-induced changes in ion fluxes across membranes, followed by establishment of an oscillation of intracellular Ca 2+ concentration, point to the involvement of a receptor Cited by: