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Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

ABSTRACT: Nowadays, plant cysteine proteinase inhibitors "namely phytocystatins" have attracted researchers towards the identification of their molecular structures and novel physiological functions. Their important roles in plant developmental processes and different stress responses have been well known. In spite of advances in the understanding of phytocystatins, we lack enough data concerning their heterologous expression especially in the forms of fusion products that are most important whether for biochemical, pharmacological or clinical studies. The present work describes an easy method of expression, purification and functional characterization in Escherichia coli of maize cystatin as a part of maltose-binding fusion protein. Assessments revealed that upon expression of fused product the total antioxidation status of the induced recombinant cells is increased. This result leads to question 'Is there any parallel functional correlation between anti-proteolytic and anti-oxidative systems?' However, the present research will open a gate for the new studies regarding the putative communicative roles of these systems that may be existing in the biological world.

SUBMITTER: Gholizadeh A

PROVIDER: S-EPMC3550510 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

Gholizadeh Ashraf A

Physiology and molecular biology of plants : an international journal of functional plant biology 20120701 3

Nowadays, plant cysteine proteinase inhibitors "namely phytocystatins" have attracted researchers towards the identification of their molecular structures and novel physiological functions. Their important roles in plant developmental processes and different stress responses have been well known. In spite of advances in the understanding of phytocystatins, we lack enough data concerning their heterologous expression especially in the forms of fusion products that are most important whether for b ...[more]

PMID: 23814438

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Project description:Proteins secreted by the type V secretion system possess multiple functions, including the capacity to mediate adhesion, aggregation, and biolfilm formation. The type V secretion system can be divided into five subclasses, one of which is the type Ve system. Proteins of the type Ve secretion system are also referred to as inverse autotransporters (IATs). In this study, we performed an in silico analysis of 126 completely sequenced Escherichia coli genomes available in the NCBI database and identified several distinct IAT-encoding gene families whose distribution varied throughout the E. coli phylogeny. The genes included three characterized IATs (intimin, fdeC, and yeeJ) and four uncharacterized IATs (here named iatA, iatB, iatC, and iatD). The four iat genes were cloned from the completely sequenced environmental E. coli strain SMS-3-5 and characterized. Three of these IAT proteins (IatB, IatC, and IatD) were expressed at the cell surface and possessed the capacity to mediate biofilm formation in a recombinant E. coli K-12 strain. Further analysis of the iatB gene, which showed a unique association with extraintestinal E. coli strains, suggested that its regulation is controlled by the LeuO global regulator. Overall, this study provides new data describing the prevalence, sequence variation, domain structure, function, and regulation of IATs found in E. coliIMPORTANCEEscherichia coli is one of the most prevalent facultative anaerobes of the human gut. E. coli normally exists as a harmless commensal but can also cause disease following the acquisition of genes that enhance its pathogenicity. Adhesion is an important first step in colonization of the host and is mediated by an array of cell surface components. In E. coli, these include a family of adhesins secreted by the type V secretion system. Here, we identified and characterized new proteins from an emerging subclass of the type V secretion system known as the inverse autotransporters (IATs). We found that IAT-encoding genes are present in a wide range of strains and showed that three novel IATs were localized on the E. coli cell surface and mediated biofilm formation. Overall, this study provides new insight into the prevalence, function, and regulation of IATs in E. coli.

Dataset Information

Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

Publications

Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

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