2011
DOI: 10.1007/s10930-011-9335-z
|View full text |Cite
|
Sign up to set email alerts
|

Structural Insights on Two Hypothetical Secretion Chaperones from Xanthomonas axonopodis pv. citri

Abstract: Several Gram-negative bacterial pathogens have developed type III secretion systems (T3SSs) to deliver virulence proteins directly into eukaryotic cells in a process essential for many diseases. The type III secretion processes require customized chaperones with high specificity for binding partners, thus providing the secretion to occur. Due to the very low sequence similarities among secretion chaperones, annotation and discrimination of a great majority of them is extremely difficult and a task with low sco… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
4
0

Year Published

2013
2013
2021
2021

Publication Types

Select...
5
1

Relationship

2
4

Authors

Journals

citations
Cited by 7 publications
(4 citation statements)
references
References 57 publications
0
4
0
Order By: Relevance
“…The UV-Vis spectrum displays two main bands, an SPR band at 440 nm, characteristic of the AgNP presence, and an additional band at 280 nm, which could be attributed to the aromatic amino acids of the capping proteins [ 69 ]. It is well-known that the absorption band in this region arises due to the electronic excitations in tryptophan, tyrosine and/or phenylalanine residues in fungal proteins [ 69 71 ]. These results confirm the AgNPs formation and the presence of fungal proteins.…”
Section: Resultsmentioning
confidence: 99%
“…The UV-Vis spectrum displays two main bands, an SPR band at 440 nm, characteristic of the AgNP presence, and an additional band at 280 nm, which could be attributed to the aromatic amino acids of the capping proteins [ 69 ]. It is well-known that the absorption band in this region arises due to the electronic excitations in tryptophan, tyrosine and/or phenylalanine residues in fungal proteins [ 69 71 ]. These results confirm the AgNPs formation and the presence of fungal proteins.…”
Section: Resultsmentioning
confidence: 99%
“…citri (Xac) proteins, a virulent Gram-negative pathogen that causes citrus canker disease. [11][12][13] These bacteria enter into the host-plant through the stomata, and through an impressive arsenal of proteins, including pectinases and celullases, cause visible circular spot-wounds. 14 Several bacteria and fungi have been reported to produce cocktails of hydrolytic depolymerising lignocellulosic enzymes and usually fungi are considered a better option in terms of enzyme varieties and yields.…”
Section: Introductionmentioning
confidence: 99%
“…This protein also was characterized as one of the most abundant proteins in outer membrane vesicles of X. citri [ 50 ] and it is secreted only by the hrpB4 mutant grown in XAM1 medium [ 41 ]. AKJ12_17400 is homologous to XAC0419, annotated as HPF/RaiA family ribosome-associated protein in X. arboricola , a stress-response protein that binds the ribosomal subunit interface and arrests translation by interfering with aminoacyl-tRNA binding to the ribosomal A site [ 51 ]. This ribosome-associated inhibitor protein stabilizes bacterial ribosomes under stress, stationary phase, and normal growth conditions and may be correlated with T3SS [ 51 ].…”
Section: Discussionmentioning
confidence: 99%
“…AKJ12_17400 is homologous to XAC0419, annotated as HPF/RaiA family ribosome-associated protein in X. arboricola , a stress-response protein that binds the ribosomal subunit interface and arrests translation by interfering with aminoacyl-tRNA binding to the ribosomal A site [ 51 ]. This ribosome-associated inhibitor protein stabilizes bacterial ribosomes under stress, stationary phase, and normal growth conditions and may be correlated with T3SS [ 51 ]. AKJ12_14465 is a secreted protein homologous to XAC3439, a protein regulated by diffusible signal factor (DSF)/rpf genes [ 52 ].…”
Section: Discussionmentioning
confidence: 99%