Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs

Article Abstract:

Multimodular penicillin-binding proteins (PBPs) belonging to the penicilloyl serine transferases family were analyzed. The molecular evolution of PBPs gave rise to two classes, class A and class B. The n-PB cores of class A had an extended amino acid sequence signature in the form of six conserved motifs and sustained steady divergence without a distinct adaptive radiation. On the other hand, the n-PB and PB cores of class B underwent adaptive radiation in a concerted manner. Mutations of PBPs developed a two-stroke engine which decreased the affinity to beta-lactam antibiotics.

Carrier proteins, Transport proteins, Drug resistance in microorganisms, Penicillin, Penicillins

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The Escherichia coli proteome: Past, present, and future prospects

Article Abstract:

The Escherichia coli proteome is used with the advent of advanced proteomic technologies for the validation of new technologies and methodologies such as sample prefractionation, protein enrichment, protein detection and image analysis software. These technologies provide a great amount of additional information of the Escherichia coli proteome and contribute to other proteomic studies.

Usage, Mass spectrometry, Proteomics

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ISCR elements: Novel gene-capturing systems of the 21st century?

Article Abstract:

Common regions (CRs) are renamed as ISCR to give a more accurate reflection of their functional properties and they are increasingly linked to mega-antibiotic-resistant regions. The genetic context surrounding ISCRs elements shows that they procure 5' sequences through misreading of the cognate termination sites.

Base sequence, Structure

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