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1.
J Exp Bot ; 75(8): 2235-2245, 2024 Apr 15.
Article in English | MEDLINE | ID: mdl-38262702

ABSTRACT

Most legumes can form an endosymbiotic association with soil bacteria called rhizobia, which colonize specialized root structures called nodules where they fix nitrogen. To colonize nodule cells, rhizobia must first traverse the epidermis and outer cortical cell layers of the root. In most legumes, this involves formation of the infection thread, an intracellular structure that becomes colonized by rhizobia, guiding their passage through the outer cell layers of the root and into the newly formed nodule cells. In this brief review, we recount the early research milestones relating to the rhizobial infection thread and highlight two relatively recent advances in the symbiotic infection mechanism, the eukaryotically conserved 'MYB-AUR1-MAP' mitotic module, which links cytokinesis mechanisms to intracellular infection, and the discovery of the 'infectosome' complex, which guides infection thread growth. We also discuss the potential intertwining of the two modules and the hypothesis that cytokinesis served as a foundation for intracellular infection of symbiotic microbes.


Subject(s)
Fabaceae , Rhizobium , Fabaceae/microbiology , Bacteria , Symbiosis , Root Nodules, Plant
3.
Proc Natl Acad Sci U S A ; 119(43): e2202606119, 2022 10 25.
Article in English | MEDLINE | ID: mdl-36252014

ABSTRACT

The subcellular events occurring in cells of legume plants as they form transcellular symbiotic-infection structures have been compared with those occurring in premitotic cells. Here, we demonstrate that Aurora kinase 1 (AUR1), a highly conserved mitotic regulator, is required for intracellular infection by rhizobia in Medicago truncatula. AUR1 interacts with microtubule-associated proteins of the TPXL and MAP65 families, which, respectively, activate and are phosphorylated by AUR1, and localizes with them within preinfection structures. MYB3R1, a rhizobia-induced mitotic transcription factor, directly regulates AUR1 through two closely spaced, mitosis-specific activator cis elements. Our data are consistent with a model in which the MYB3R1-AUR1 regulatory module serves to properly orient preinfection structures to direct the transcellular deposition of cell wall material for the growing infection thread, analogous to its role in cell plate formation. Our findings indicate that the eukaryotically conserved MYB3R1-TPXL-AUR1-MAP65 mitotic module was conscripted to support endosymbiotic infection in legumes.


Subject(s)
Aurora Kinases , Medicago truncatula , Plant Proteins , Rhizobium , Symbiosis , Aurora Kinases/genetics , Aurora Kinases/metabolism , Gene Expression Regulation, Plant , Medicago truncatula/genetics , Medicago truncatula/microbiology , Microtubule-Associated Proteins/metabolism , Plant Proteins/genetics , Plant Proteins/metabolism , Rhizobium/metabolism , Transcription Factors/metabolism
4.
Curr Biol ; 31(16): 3538-3550.e5, 2021 08 23.
Article in English | MEDLINE | ID: mdl-34216556

ABSTRACT

The establishment of the symbiotic interaction between rhizobia and legumes involves the Nod factor signaling pathway. Nod factor recognition occurs through two plant receptors, NFR1 and NFR5. However, the signal transduction mechanisms downstream of NFR1-NFR5-mediated Nod factor perception remain largely unknown. Here, we report that a small guanosine triphosphatase (GTPase), GmROP9, and a guanine nucleotide exchange factor, GmGEF2, are involved in the soybean-rhizobium symbiosis. We show that GmNFR1α phosphorylates GmGEF2a at its N-terminal S86, which stimulates guanosine diphosphate (GDP)-to-GTP exchange to activate GmROP9 and that the active form of GmROP9 can associate with both GmNFR1α and GmNFR5α. We further show that a scaffold protein, GmRACK1, interacts with active GmROP9 and contributes to root nodule symbiosis. Collectively, our results highlight the symbiotic role of GmROP9-GmRACK1 and support the hypothesis that rhizobial signals promote the formation of a protein complex comprising GmNFR1, GmNFR5, GmROP9, and GmRACK1 for symbiotic signal transduction in soybean.


Subject(s)
Glycine max , Plant Root Nodulation , Rhizobium , Signal Transduction , Gene Expression Regulation, Plant , Plant Proteins/genetics , Plant Proteins/metabolism , Rhizobium/physiology , Glycine max/microbiology , Glycine max/physiology , Symbiosis
5.
Acta Biochim Biophys Sin (Shanghai) ; 38(9): 611-9, 2006 Sep.
Article in English | MEDLINE | ID: mdl-16953299

ABSTRACT

When manganese stabilizing protein (MSP) was treated with 0.5 mM N-succinimidyl propionate (NSP), the rebinding ability and oxygen-releasing capabilities of the modified MSP were not altered, in spite of changes of MSP surface Lys residues. Furthermore, far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed that 0.5 mM NSP-modified MSP retained most of its native secondary and tertiary structure. Mapping of the sites of NSP modification by Staphylococcus V(8) protease digestion of the modified protein, as well as analysis by matrix-assisted laser desorption ionization-time of flight mass spectrometry, indicated that seven Lys residues were modified. The results suggested that these residues are not absolutely essential to the structure and function of MSP. However, when the NSP concentration was increased to 4 mM, the modified MSP was unable to bind photosystem II and completely lost its reactivating capability. Both far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed a clear conformational change in MSP after 4 mM NSP treatment, suggesting that some Lys residues are involved in maintaining the structure and function of MSP. Analysis by matrix-assisted laser desorption ionization-time of flight mass spectrometry indicated that another six Lys residues, namely Lys20, Lys101, Lys196, Lys207, Lys130 (or Lys137) and Lys66 (or Lys76), were modified by 4 mM NSP. Therefore, these six Lys residues are crucial in maintaining the structure and function of soluble MSP.


Subject(s)
Lysine/chemistry , Photosystem II Protein Complex/chemistry , Binding Sites , Protein Binding , Solubility , Structure-Activity Relationship
6.
Article in Chinese | MEDLINE | ID: mdl-16361782

ABSTRACT

This review describes the recent progress in understanding of light harvesting complexes and reaction centers from purple bacteria. Emphasis is paid on the structure of two light harvesting complexes, inner or outer, and the mechanism of the transfer of excited energy among relative pigments (Fig.1). At the same time, it is detailedly stated about the understanding of the structure of the reaction center and the transform mechanism from light energy to chemical energy, usable for life system (Fig.2).


Subject(s)
Bacterial Proteins/metabolism , Light-Harvesting Protein Complexes/metabolism , Proteobacteria/metabolism , Bacterial Proteins/chemistry , Light-Harvesting Protein Complexes/chemistry , Models, Biological
7.
Acta Biochim Biophys Sin (Shanghai) ; 37(11): 737-42, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16270152

ABSTRACT

To determine the contribution of charged amino acids to binding with the photosystem II complex (PSII), the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with N-succinimidyl propionate (NSP) or glycine methyl ester (GME) in the presence of a water-soluble carbodiimide, respectively. Based on isoelectric point shift, 4-10 and 10-14 amino groups were modified in the presence of 2 and 4 mM NSP, respectively. Similarly, 3-4 carboxyl groups were modified by reaction with 100 mM GME. Neutralization of negatively charged carboxyl groups with GME did not alter the binding activity of the extrinsic 18 kDa protein. However, the NSP-modified 18 kDa protein, in which the positively charged amino groups had been modified to uncharged methyl esters, failed to bind with the PSII membrane in the presence of the extrinsic 23 kDa protein. This defect can not be attributed to structural or conformational alterations imposed by chemical modification, as the fluorescence and circular dichroism spectra among native, GME- and NSP-modified extrinsic 18 kDa proteins were similar. Thus, we have concluded that the positive charges of lysyl residues in the extrinsic 18 kDa protein are important for its interaction with PSII membranes in the presence of the extrinsic 23 kDa protein. Furthermore, it was found that the negative charges of carboxyl groups of this protein did not participate in binding with the extrinsic 23 kDa protein associated with PSII membranes.


Subject(s)
Cell Membrane/chemistry , Glycine/analogs & derivatives , Lysine/chemistry , Photosystem II Protein Complex/chemistry , Propionates/chemistry , Spinacia oleracea/chemistry , Binding Sites , Glycine/chemistry , Molecular Weight , Protein Binding , Static Electricity
8.
Article in Chinese | MEDLINE | ID: mdl-15599051

ABSTRACT

Experiments were carried out with cotton (Gossgpium hirsutum cv. Xuzhou 142) plants to study the effects of illumination with xenon and sulfur lamp on development of cotton plants. The results showed that, compared with xenon lamp, illumination with sulfur lamp inhibited excessive elongation of hypocotyl via promotion of longitudinal elongation of epidermis and cortex cells, increased the numbers of branches, buds and bolls significantly. It suggested that illumination with sulfur lamp rendered cotton photomorphogenesis more favorable to yield formation.


Subject(s)
Gossypium/growth & development , Sulfur/pharmacology , Xenon/pharmacology , Light
9.
Article in Chinese | MEDLINE | ID: mdl-15643091

ABSTRACT

The primary mechanism of growth difference of cucumber (Cucumis sativus L.) seedlings cultured under sulfur lamp and xenon lamp in a phytotron was investigated. Compared with cucumber seedlings grown under xenon lamp, those under sulfur lamp were shorter, and the cell number in the middle hypocotyls epidermis and cortex of them were more (Fig. 1, Table 1). Endogenous hormone analysis indicates that the content of IAA and GA(3) of seedlings under sulfur lamp were 17% and 24% lower, while ABA content was 31% higher than that under xenon lamp (Fig. 2). Based on these results, it is suggested that the growth difference between cucumber seedlings grown under sulfur lamp and under xenon lamp might be related to the control of endogenous hormones.


Subject(s)
Cucumis sativus/metabolism , Cucumis sativus/radiation effects , Light , Plant Growth Regulators/metabolism , Seedlings/metabolism , Seedlings/radiation effects , Sulfur , Xenon , Cucumis sativus/growth & development , Gene Expression Regulation, Plant/radiation effects , Seedlings/growth & development
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