Substrate recognition by the Yersinia type III protein secretion machinery

Ramamurthi, Kumaran S.; Schneewind, Olaf

doi:10.1046/j.1365-2958.2003.03777.x

Cited by 48 publications

(44 citation statements)

References 48 publications

(85 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The toxin hemolysin A in E. coli is secreted by the type I system (Sec independent) and has a C-terminal signal sequence localized in the last 50 -60 residues of the protein. The components of the type III secretion pathway, primarily in Gram-negative pathogenic bacteria, share sequence homology with the components of the flagellar body (29). Interestingly, both hemolysin, and the flagellin protein FliC, were among the highest (of the low) scores in BLASTP similarity searches performed with WspA.…”

Section: Discussionmentioning

confidence: 99%

UV Irradiation and Desiccation Modulate the Three-dimensional Extracellular Matrix of Nostoc commune (Cyanobacteria)

Wright

Smith

Joardar

et al. 2005

Journal of Biological Chemistry

112

105

View full text Add to dashboard Cite

Cyanobacterium Nostoc commune can tolerate the simultaneous stresses of desiccation, UV irradiation, and oxidation. Acidic WspA, of ϳ33.6 kDa, is secreted to the three-dimensional extracellular matrix and accounts for greater than 70% of the total soluble protein. The wspA gene of N. commune strain DRH1 was cloned and found in a single genomic copy, in a monocistronic operon. Transcription of wspA and sodF (superoxide dismutase), and synthesis and secretion of WspA, were induced upon desiccation or UV-A/B irradiation of cells. Recombinant WspA binds the UV-A/B absorbing pigment scytonemin through non-covalent interactions. WspA peptide polymorphism, and heterogeneity of multiple wspA sequences within cells of a single colony, account for distinct WspA isoforms. WspA has no similarity to entries in the sequence databases and wspA, a possible xenolog, is restricted to a subset of strains in the "form species" N. commune characterized through group I intron phylogeny. We hypothesize that WspA plays a central role in the global stress response of N. commune through modulation of the structure and function of the three-dimensional extracellular matrix, particularly the transport, distribution, and/or macromolecular architecture of mycosporine and scytonemin UV-A/B absorbing pigment complexes.Cyanobacteria make a major contribution to world photosynthesis and nitrogen fixation, but their dense and often toxic "blooms" in marine, brackish, and fresh waters are of growing concern to public health (1). The sequences of a wide range of cyanobacterial genomes are becoming available and constitute an important resource both for the rational management and exploitation of these organisms, as well as the study of topics as diverse as carbon fixation, cell differentiation, plant and fungal symbioses, secondary product biosynthesis, and evolution.

show abstract

Section: Discussionmentioning

confidence: 99%

UV Irradiation and Desiccation Modulate the Three-dimensional Extracellular Matrix of Nostoc commune (Cyanobacteria)

Wright

Smith

Joardar

et al. 2005

Journal of Biological Chemistry

112

105

View full text Add to dashboard Cite

show abstract

“…There is little consensus between secretion signals of different bacteria, and it is thought that the protein sequence of these N-terminal secretion signals possesses a common secondary structure that allows proteins to be recruited to the T3SS (Stebbins, 2005). However, the fact that frameshift mutations of the DNA sequence corresponding to the first 15 amino acids of certain effectors still allow protein secretion has led others to propose an RNA-mediated secretion signal for transcripts of effectors to be recruited and effectors to be translated and secreted simultaneously (Ramamurthi & Schneewind, 2003;Sorg et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Secretion and translocation signals and DspB/F-binding domains in the type III effector DspA/E of Erwinia amylovora

Carpenter

Hayes

et al. 2010

Microbiology

View full text Add to dashboard Cite

DspA/E is a type III effector of Erwinia amylovora, the bacterial pathogen that causes fire blight disease in roseaceous plants. This effector is indispensable for disease development, and it is translocated into plant cells. A DspA/E-specific chaperone, DspB/F, is necessary for DspA/E secretion and possibly for its translocation. In this work, DspB/F-binding sites and secretion and translocation signals in the DspA/E protein were determined. Based on yeast two-hybrid assays, DspB/F was found to bind DspA/E within the first 210 amino acids of the protein. Surprisingly, both DspB/F and OrfA, the putative chaperone of Eop1, also interacted with the C-terminal 1059 amino acids of DspA/E; this suggests another chaperone-binding site. Secretion and translocation assays using serial N-terminal lengths of DspA/E fused with the active form of AvrRpt2 revealed that at least the first 109 amino acids, including the first N-terminal chaperone-binding motif and DspB/F, were required for efficient translocation of DspA/E, although the first 35 amino acids were sufficient for its secretion and the presence of DspB/F was not required. These results indicate that secretion and translocation signals are present in the N terminus of DspA/E, and that at least one DspB/F-binding motif is required for efficient translocation into plant cells.

show abstract

“…Previous work examined the secretion signals of Yop proteins (Lloyd et al, 2001a;Cornelis, 2003;Ramamurthi and Schneewind, 2003a). YopE harbours multiple sequence elements that impact its secretion.…”

Section: Discussionmentioning

confidence: 99%

“…For both effector Yops, isoleucine at position 3 has been described as an essential residue for substrate recognition by the type III machinery (Ramamurthi and Schneewind, 2003a). For example, the first seven codons of YopE have been shown to promote secretion of a fused neomycin phosphotransferase (Npt) reporter (Ramamurthi and Schneewind, 2005).…”

Section: Minimal Secretion Signals In Post-translational Transport Ofmentioning

confidence: 99%

“…Secretion signals for several Yops have been mapped (Cornelis, 2003;Ramamurthi and Schneewind, 2003a). Translational hybrids between YopE and Npt, neomycin phosphotransferase, generated hybrid proteins that were secreted under low calcium conditions or injected into the cytosol of mammalian cells (Sory and Cornelis, 1994;Sory et al, 1995;Anderson and Schneewind, 1997;Lee et al, 1998).…”

Section: Synthesis and Secretion Of Yop Proteins Occurs Whenmentioning

confidence: 99%

See 1 more Smart Citation

Ubiquitin‐Yop hybrids as probes for post‐translational transport by the Yersinia type III secretion pathway

Quenee

Schneewind²

2007

Molecular Microbiology

Self Cite

View full text Add to dashboard Cite

SummaryYersinia enterocolitica uses type III secretion to transport Yop proteins into the cytoplasm of host cells. Previous work generated hypotheses for both co-and post-translational transport mechanisms in the Yersinia type III pathway. Here, we used ubiquitin (Ub) and UBP1, the Ub-specific protease, to examine whether Yops can be secreted when synthesized prior to recognition by the type III machinery. Fusion of Ub to the N-terminus of Yops blocked substrate recognition and secretion of hybrids generated with YopE, YopQ or YopR. UBP1 removed Ub from the N-terminus of these hybrids and allowed YopE, YopQ or YopR cleavage products to enter the secretion pathway. Following the release of Ub, Yersinia type III machines also transported the YopE cleavage product into the cytosol of tissue culture cells. Minimal secretion signals were also examined with the Ub/UBP1 system and some, but not all, of these signals promoted type III secretion even after polypeptides had been freed from Ub. These results suggest that recognition and secretion of Yop substrates by the type III machinery can occur by a post-translational mechanism.

show abstract

Substrate recognition by the Yersinia type III protein secretion machinery

Cited by 48 publications

References 48 publications

UV Irradiation and Desiccation Modulate the Three-dimensional Extracellular Matrix of Nostoc commune (Cyanobacteria)

UV Irradiation and Desiccation Modulate the Three-dimensional Extracellular Matrix of Nostoc commune (Cyanobacteria)

Secretion and translocation signals and DspB/F-binding domains in the type III effector DspA/E of Erwinia amylovora

Ubiquitin‐Yop hybrids as probes for post‐translational transport by the Yersinia type III secretion pathway

Contact Info

Product

Resources

About