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Ruth Nussinov, NCI-Frederick, discusses the possible mechanisms that support long-range signalling in cells in this hot Opinion article. This paper proposes that conformational disorder can help faster propagation of signals across the cell. This article is part of our themed issue on intrinsically disordered proteins and is currently free to access for 4 weeks.
The first of the International Symposia on Advancing the Chemical Sciences (ISACS) series next year is to be Challenges in Organic Chemistry and Chemical Biology (ISACS7) on 12 – 15 June at the University of Edinburgh, UK. See the excellent list of confirmed speakers and details of the abstract submission process here. Late embryogenesis abundant (LEA) proteins are intrinsically disordered proteins (IDPs) with a role in limiting the aggregation of proteins in cells that are exposed to water loss.  In this hot article Sohini Chakrabortee et al. Some intrinsically disordered proteins associated with desiccation tolerance have a novel function: they behave as molecular shields, reducing the rate of aggregation of other, aggregation-prone proteins. Roger Linington, senior author on the paper, nominated the team for the award, “I feel that this awards highlights some of the high quality interdisciplinary research being fostered by the UCSC Chemical Screening Center.
The hot article on the cover of this month’s issue is from Andreas Keller and Christina Backes et al. Andreas Keller, Christina Backes, Petra Leidinger, Nathalie Kefer, Valesca Boisguerin, Catalin Barbacioru, Britta Vogel, Mark Matzas, Hanno Huwer, Hugo A. View the rest of Issue 12, including hot articles on predicting antibody complementarity and how fluorescent labelling agents change binding profiles of glycan-binding proteins. The complementarity determining regions (CDRs) in antibodies define the majority of their antigen binding functionality, and as such have been well studied and classified.  Here it is shown that CDR structure can be predicted in the same way as standard loop structures using FREAD, a successful database loop prediction technique. Andreas Keller, Christina Backes, Petra Leidinger, Nathalie Kefer, Valesca Boisguerin, Catalin Barbacioru, Britta Vogel, Mark Matzas, Hanno Huwer, Hugo A. In this hot review Johnny Habchi and Sonia Longhi discuss intrinsically disordered proteins in a number of viruses – the Nipah, Hendra and measles viruses of the Paramyxoviridae family. Difficulty in obtaining high-resolution structural data has so far limited understanding of the amount and role of disorder in the viral proteins, but recent research has uncovered that the nucleo- and phosphoproteins contain disordered regions up to 400 residues long.  Using computational approaches they extend these results to the rabies virus and respiratory syncytial virus, showing that structural disorder is conserved and widespread throughout the two viral families.
In the last few years there has been a growing interest towards intrinsically disordered proteins related to the understanding of the numerous and diverse functional roles they play. This article is part of our forthcoming themed issue on intrinsically disordered proteins – check back soon for more hot articles in this issue!


On the cover of our latest issue is work from Minkui Luo and team at the Memorial Sloan-Kettering Cancer Center, New York. They have developed a high throughput format of a fluorogenic assay to screen for protein methyltransferase (PMT) activity and demonstrate its applicability by  screening 8 human PMTs with SAM as a cofactor and 5 SAM analogues.  The authors hope the SAR information obtained will provide additional guidance to engineer PMTs and matched SAM analogues for more efficient substrate labelling, and that the assay will be useful for probing activities and screening inhibitors of methyltransferase and SAM variants. Bisphosphonates are used in 99mTc-based radiopharmaceuticals for bone imaging, and have been successful in the treatment of conditions characterized by increased osteoclast-mediated bone resorption, such as Paget’s disease, osteoporosis and tumor bone disease. This hot review from Isabel Santos and colleagues at the Unit of Chemical and Radiopharmaceutical Sciences, Portugal, collates the most recent information on the synthesis, characterization and biological evaluation of novel bisphosphonate-containing radiopharmaceauticals for imaging or therapy of bone-related diseases. Regis Grailhe and colleagues from the Institut Pasteur Korea have investigated the relative merits of commonly used techniques for analysing protein-protein interactions using a small network of Alzheimer related proteins involved in amyloid ? production as a case study.
They used fluorescence resonance energy transfer (FRET), bioluminescence resonance energy transfer (BRET) and fluorescence lifetime imaging microscopy (FLIM) to detect interactions, finding a previously unreported interacting pair and concluding that FRET based cytometry was the most sensitive and reliable approach to screen for new interacting proteins. In this article, molecular shields are shown to be distinct from molecular chaperones, instead resembling polymeric stabilisers of colloidal suspensions and implicating a role in stabilisation of the cell cytoplasm during water stress. It is a testament to the value of cross-specialization projects such as this that the results were chosen for this award by the qb3 community. FREAD is able to predict CDR loops accurately and without classification, to account for structural changes of CDRs on binding the antigens. Our group played a pioneering role in focusing the attention of virologists on the abundance of disorder within proteins of the replicative complex of paramyxoviruses. Dense packing facilitates efficient transmission of the allosteric energy wave, which leads to fast cellular response to external stimuli. Following these seminal reports in the early 2000s, many other studies that addressed the disordered nature of various viral proteins have been published in subsequent years, leading to revisiting the classical way structure-function relationships in viral proteins are seen. The main advantage of disorder within viral proteins has been proposed to be related to (i) mutational robustness, (ii) pleiotropy, (iii) genetic compaction and (iv) the lessening of evolutionary constraints on overlapping reading frames. In the coming years we aim at further extending these studies by assessing the disordered state of disordered regions from paramyxoviral proteins in the context of intact nucleocapsids as well as in the context of infected cells so as to achieve a more realistic description of the behavior and functional impact of these regions. At the same time we will focus on the identification of small compounds able to block crucial protein-protein interactions mediated by disordered regions and to the assessment of their mechanism of action both in vitro and in vivo.



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09.11.2015, author: admin


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