Protein moonlighting: what is it, and why is it important?
TLDR
Members of the GroEL/HSP60 protein family have been studied for many years because of their critical roles as ATP-dependent molecular chaperones, so it might come as a surprise that some have important functions in ATP-poor conditions.Abstract:
Members of the GroEL/HSP60 protein family have been studied for many years because of their critical roles as ATP-dependent molecular chaperones, so it might come as a surprise that some have important functions in ATP-poor conditions, for example, when secreted outside the cell. At least some members of each of the HSP10, HSP70, HSP90, HSP100 and HSP110 heat shock protein families are also 'moonlighting proteins'. Moonlighting proteins exhibit more than one physiologically relevant biochemical or biophysical function within one polypeptide chain. In this class of multifunctional proteins, the multiple functions are not due to gene fusions or multiple proteolytic fragments. Several hundred moonlighting proteins have been identified, and they include a diverse set of proteins with a large variety of functions. Some participate in multiple biochemical processes by using an active site pocket for catalysis and a different part of the protein's surface to interact with other proteins. Moonlighting proteins play a central role in many diseases, and the development of novel treatments would be aided by more information addressing current questions, for example, how some are targeted to multiple cellular locations and how a single function can be targeted by therapeutics without targeting a function not involved in disease.This article is part of the theme issue 'Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective'.read more
Citations
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Paraprobiotics and Postbiotics of Probiotic Lactobacilli, Their Positive Effects on the Host and Action Mechanisms: A Review.
Tsegay Teame,Anran Wang,Mingxu Xie,Zhen Zhang,Yalin Yang,Qianwen Ding,Chenchen Gao,Rolf Erik Olsen,Chao Ran,Zhigang Zhou +9 more
TL;DR: This review systematically summarize the paraprobiotics and postbiotics derived from Lactobacilli and their beneficial functions, and discusses the mechanisms underlying their beneficial effects on the host, and their interaction with the host cells.
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Extracellular cell stress (heat shock) proteins-immune responses and disease: an overview.
TL;DR: The burgeoning literature reporting the presence of stress proteins in a range of biological fluids in healthy individuals/non-diseased settings, the association of extracellular stress protein levels with a plethora of clinical and pathological conditions and the selective expression of a membrane form of Hsp70 on cancer cells now supports the concept that cell stress proteins are involved in maintaining/regulating organismal homeostasis and in disease processes and phenotype.
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The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.
TL;DR: The structural studies indicate that short linear motifs in surface exposed, non-conserved regions of the molecule may play a key role in the moonlighting functions ascribed to this ancient, highly abundant protein.
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Understudied proteins: opportunities and challenges for functional proteomics
Georg Kustatscher,Tom Collins,Anne-Claude Gingras,Tiannan Guo,Henning Hermjakob,Trey Ideker,Kathryn S. Lilley,Emma Lundberg,Edward M. Marcotte,Markus Ralser,Juri Rappsilber +10 more
TL;DR: The Understudied Protein Initiative as discussed by the authors aims to reduce the annotation gap by systematically associating uncharacterized proteins with proteins of known function, thereby laying the groundwork for future detailed mechanistic studies.
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Bacterial Excretion of Cytoplasmic Proteins (ECP): Occurrence, Mechanism, and Function.
Patrick Ebner,Friedrich Götz +1 more
TL;DR: The excretion of cytoplasmic and signal-peptide-less proteins (ECP) by microorganisms and eukaryotes remains a fascinating topic and some CPs might be promising candidates for vaccine developments against major bacterial pathogens.
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