Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool

Ciragan, Annika; Aranko, A. Sesilja; Tascón, Igor; Iwaï, Hideo

doi:10.1016/j.jmb.2016.10.006

Cited by 41 publications

(77 citation statements)

References 59 publications

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“…Therefore, β6-strand in Ec TonB-137 NMR structure has to be exchanged with the strand in TonB box when interacting with TBDTs (Peacock et al, 2005). In contrast, the recent solution NMR structure of the last 92 residues from Helicobacter pyroli TonB ( Hp TonB-92) showed the disordered C-terminal region and the absence of β6-strand (Ciragan et al, 2016), which is more in line with the crystal structures of Ec TonB-CTD reported previously (Ködding et al, 2005; Shultis et al, 2006;Pawelek et al, 2006). …”

Section: Introductionsupporting

confidence: 83%

“…The solution NMR structure of Pa TonB-96 elucidated in this work is accessible to the TonB box without the strand exchange, because the disordered and extended C-terminal end does not interfere with the interaction site. This open conformation at the C-terminus is also observed in the NMR structures of Hp TonB-92 (Ciragan et al, 2016) and TonB-like protein, HasB from Serratia marcescens (Amorim et al, 2013). Thus it might be a more common structure among CTDs of TonB proteins across different organisms.…”

Section: Discussionmentioning

confidence: 55%

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NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Oeemig

Ollila

Iwaï

2018

PeerJ

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The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. Several distinct conformations of differently dissected CTDs of Escherichia coli TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of Pseudomonas aeruginosa TonB (PaTonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338–342), different from the NMR structure of E. coli TonB (EcTonB-137). The extended and flexible C-terminal residues are confirmed by 15N relaxation analysis and molecular dynamics simulation. We created models for the PaTonB-96/TonB box interaction and propose that the internal fluctuations of PaTonB-96 makes it more accessible for the interactions with the TonB box and possibly plays a role in disrupting the plug domain of the TonB-dependent OM transporters.

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Section: Introductionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 55%

NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Oeemig

Ollila

Iwaï

2018

PeerJ

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“…1A) [1]. Even though the solubility issue of the precursors fused to split intein fragments has been recently alleviated by highly soluble inteins from halophilic organisms, preparations of individual split intein fusions are mandatory [12]. Protein ligation by protein trans-splicing (PTS) via split inteins or split HINT domains is not restricted by Cys residue at the ligation junction (Fig.…”

mentioning

confidence: 99%

Segmental isotopic labeling of a single‐domain globular protein without any refolding step by an asparaginyl endopeptidase

et al. 2017

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Asparaginyl endopeptidases (AEPs) catalyze head-to-tail backbone cyclization of naturally occurring cyclic peptides such as cyclotides, and have become an important peptide-engineering tool for macrocyclization and peptide ligation. Here, we report efficient protein ligation in trans by mimicking efficient backbone cyclization by an AEP without any excess of reactants. We demonstrate a practical application of segmental isotopic labeling for NMR studies of a single-domain globular protein without any refolding step using the recombinant AEP prepared from Escherichia coli. This simple protein ligation approach using an AEP could be applied for incorporation of various biophysical probes into proteins as well as post-translational production of full-length proteins.

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“…It would thus seem that the use of intein processing as an environmental sensor represents a strategy designed to prevent activation of a protein when the cell is undergoing stress. Moreover, as intein processing is an irreversible reaction, it can be assumed that this protein processing scheme represents a so‐called “panic button.” At the same time, condition‐dependent intein processing carries considerable applied potential, particularly when the dependency on appropriate conditions is engineered into biotechnologically relevant proteins, other than those where such post‐translational modification naturally occurs …”

Section: Inteins—an Irreversible Ptm That Can Occur In Response To Enmentioning

confidence: 99%

Modifying Post‐Translational Modifications: A Strategy Used by Archaea for Adapting to Changing Environments?

Eichler

2020

BioEssays

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In concert with the selective pressures affecting protein folding and function in the extreme environments in which they can exist, proteins in Archaea have evolved to present permanent molecular adaptations at the amino acid sequence level. Such adaptations may not, however, suffice when Archaea encounter transient changes in their surroundings. Post‐translational modifications offer a rapid and reversible layer of adaptation for proteins to cope with such situations. Here, it is proposed that Archaea further augment their ability to survive changing growth conditions by modifying the extent, position, and, where relevant, the composition of different post‐translational modifications, as a function of the environment. Support for this hypothesis comes from recent reports describing how patterns of protein glycosylation, methylation, and other post‐translational modifications of archaeal proteins are altered in response to environmental change. Indeed, adjusting post‐translational modifications as a means to cope with environmental variability may also hold true beyond the Archaea.

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Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool

Cited by 41 publications

References 59 publications

NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Segmental isotopic labeling of a single‐domain globular protein without any refolding step by an asparaginyl endopeptidase

Modifying Post‐Translational Modifications: A Strategy Used by Archaea for Adapting to Changing Environments?

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