Phage Display and Crystallographic Analysis Reveals Potential Substrate/Binding Site Interactions in the Protein Secretion Chaperone CsaA from Agrobacterium tumefaciens

Feldman, Anat R.; Shapova, Y.A.; Wu, Sampson; Oliver, David C.; Heller, Markus; McIntosh, Lawrence P.; Scott, Jamie K.; Paetzel, Mark

doi:10.1016/j.jmb.2008.03.048

Cited by 4 publications

(1 citation statement)

References 52 publications

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“…The biological significance of this result is underlined by the fact that a synthetic peptide derived from the identical region of a receptor which does not bind the toxin, and which differs by only a single amino acid, was unable to inhibit toxin binding, suggesting that the selected peptide had identified the toxin binding site. Other examples in which binding epitopes have been identified for different proteins include concanavalin A (Scott et al, 1992), p53 (Stephen and Lane, 1992;Lane and Stephen, 1993;Stephen et al, 1995), HLA (Hammer et al, 1992(Hammer et al, , 1993(Hammer et al, , 1994, amyloid beta (Magdesian et al, 2005), hepatitis B (Deng et al, 2007), CsaA (Feldman et al, 2008), and mdm2 (Bottger et al, 1996).…”

Section: Protein-binding Sitesmentioning

confidence: 99%

The Use of Phage Display in Neurobiology

Bradbury

2010

CP Neuroscience

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Phage display has been extensively used to study protein-protein interactions, receptor- and antibody-binding sites, and immune responses, to modify protein properties, and to select antibodies against a wide range of different antigens. In the format most often used, a polypeptide is displayed on the surface of a filamentous phage by genetic fusion to one of the coat proteins, creating a chimeric coat protein, and coupling phenotype (the protein) to genotype (the gene within). As the gene encoding the chimeric coat protein is packaged within the phage, selection of the phage on the basis of the binding properties of the polypeptide displayed on the surface simultaneously results in the isolation of the gene encoding the polypeptide. This unit describes the background to the technique, and illustrates how it has been applied to a number of different problems, each of which has its neurobiological counterparts. Although this overview concentrates on the use of filamentous phage, which is the most popular platform, other systems are also described.

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Section: Protein-binding Sitesmentioning

confidence: 99%

The Use of Phage Display in Neurobiology

Bradbury

2010

CP Neuroscience

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Uncovering the structure-function aspects of an archaeal CsaA protein

Sharma

Kumari

Goel

2021

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Navigating the structure–function–evolutionary relationship of CsaA chaperone in archaea

Sharma

Rani

Goel

2017

Critical Reviews in Microbiology

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CsaA is a protein involved in the post-translational translocation of proteins across the cytoplasmic membrane. It is considered to be a functional homolog of SecB which participates in the Sec-dependent translocation pathway in an analogous manner. CsaA has also been reported to act as a molecular chaperone, preventing aggregation of unfolded proteins. It is essentially a prokaryotic protein which is absent in eukaryotes, but found extensively in bacteria and earlier thought to be widely present in archaea. The study of phylogenetic distribution of CsaA among prokaryotes suggests that it is present only in few archaeal organisms, mainly species of Thermoplasmatales and Halobacteriales. Interestingly, the CsaA protein from these two archaeal orders cluster separately on the phylogenetic tree with CsaA from Gram-positive and Gram-negative bacteria. It, thus, appears that this protein might have been acquired in these archaeal organisms through independent horizontal gene transfer (HGT) events from different bacteria. In this review, we summarize the earlier biochemical, structural, and functional characterization studies of CsaA. We draw new insights into the evolutionary history of this protein through phylogenetic and structural comparison of bacterial CsaA with modelled archaeal CsaA from Picrophilus torridus and Natrialba magadii.

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Phage Display and Crystallographic Analysis Reveals Potential Substrate/Binding Site Interactions in the Protein Secretion Chaperone CsaA from Agrobacterium tumefaciens

Cited by 4 publications

References 52 publications

The Use of Phage Display in Neurobiology

The Use of Phage Display in Neurobiology

Uncovering the structure-function aspects of an archaeal CsaA protein

Navigating the structure–function–evolutionary relationship of CsaA chaperone in archaea

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