Subcellular localization of fad1p in saccharomyces cerevisiae: A choice at post-transcriptional level?

FAD synthase is the last enzyme in the pathway that converts riboflavin into FAD. In Saccharomyces cerevisiae, the gene encoding for FAD synthase is FAD1, from which a sole protein product (Fad1p) is expected to be generated. In this work, we showed that a natural Fad1p exists in yeast mitochondria and that, in its recombinant form, the protein is able, per se, to both enter mitochondria and to be destined to cytosol. Thus, we propose that FAD1 generates two echoforms— that is, two identical proteins addressed to different subcellular compartments. To shed light on the mechanism underlying the subcellular destination of Fad1p, the 3′ region of FAD1 mRNA was analyzed by 3′RACE experiments, which revealed the existence of (at least) two FAD1 transcripts with different 3′UTRs, the short one being 128 bp and the long one being 759 bp. Bioinformatic analysis on these 3′UTRs allowed us to predict the existence of a cis-acting mitochondrial localization motif, present in both the transcripts and, presumably, involved in protein targeting based on the 3′UTR context. Here, we propose that the long FAD1 transcript might be responsible for the generation of mitochondrial Fad1p echoform

Dance as a Risk Factor for Injuries and Development of Occupational Diseases

Ozljede i bolesti mogu znatno utjecati na stvaralačku sposobnost, kreativnost i dostignuća umjetnika. Povezanost uvjeta i načina rada s pojavom bolesti u umjetnika prepoznata je već u srednjem vijeku. Tjelesna zahtjevnost izvedbe, gdje se tijelo koristi kao instrument izražavanja, može uzrokovati ozljede i razvoj profesionalnih bolesti koje mogu dovesti do nemogućnosti umjetničke interpretacije na očekivanoj razini, prekinuti aktivnosti i onemogućiti nastavak profesionalne karijere. Plesači su jedna od skupina umjetnika/izvođača koji su izloženi specifičnim rizicima i kojima treba specifična zdravstvena zaštita, što nije moguće ostvariti bez poznavanja mehanizama nastajanja ozljeda i uvažavanja posebnosti potreba plesača. Mnogi plesači teže visokim umjetničkim i estetskim kriterijima izvedbe, pri čemu često protežu svoje tjelesne mogućnosti i izdržljivost i zanemaruju vlastita tjelesna ograničenja. Zdravstveni problemi plesača obuhvaćaju čitav niz ozljeda, profesionalnih bolesti i bolesti vezanih uz rad koji se kreću od stresa i straha od nastupa sve do poremećaja u prehrambenim navikama. Također obuhvaćaju ozljede mišićno-koštanoga sustava, sindrome prenaprezanja i trenažnoga preopterećenja koje može uzrokovati karakterističnu topološku pojavu boli, koja je često početak kroničnih zdravstvenih problema kod plesača. Navedeni zdravstveni problemi plesača sve su češće područje zanimanja liječnika različitih specijalizacija, unaprjeđenja i provođenja preventivnih programa, dijagnostičkih metoda i liječenja u tom djelu populacije.Injuries and diseases can significantly affect the creativity and artistic performance. The link between working conditions and artistic performance had been recognised as early as the medieval age. Physically demanding performance arts such as dance can sometimes result in injuries, illnesses, inability to perform, and even end artist’s career. Dancers are exposed to specific risks and in need of specific medical care. Many dancers often stretch their physical capabilities and endurance and neglect their physical limitations. Their health problems include a number of work-related illnesses that range from stress and stage fright to metabolic and nutritional disorders. They also include musculoskeletal injuries due to overload training that are often the beginning of chronic health problems

Motorized mirror assembly for beam switching

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Optimisation of trans-cinnamic acid and hydrocinnamyl alcohol production with recombinant Saccharomyces cerevisiae and identification of cinnamyl methyl ketone as a by-product

Trans-cinnamic acid (tCA) and hydrocinnamyl alcohol (HcinOH) are valuable aromatic compounds with applications in the flavour, fragrance and cosmetic industry. They can be produced with recombinant yeasts from sugars via phenylalanine after expression of a phenylalanine ammonia lyase (PAL) and an aryl carboxylic acid reductase. Here, we show that in Saccharomyces cerevisiae a PAL enzyme from the bacterium Photorhabdus luminescens was superior to a previously used plant PAL enzyme for the production of tCA. Moreover, after expression of a UDP-glucose:cinnamate glucosyltransferase (FaGT2) from Fragaria x ananassa, tCA could be converted to cinnamoyl-D-glucose which is expected to be less toxic to the yeast cells. Production of tCA and HcinOH from glucose could be increased by eliminating feedback-regulated steps of aromatic amino acid biosynthesis and diminishing the decarboxylation step of the competing Ehrlich pathway. Finally, an unknown by-product resulting from further metabolisation of a carboligation product of cinnamaldehyde (cinALD) with activated acetaldehyde, mediated by pyruvate decarboxylases, could be identified as cinnamyl methyl ketone providing a new route for the biosynthesis of precursors, such as (2S,3R) 5-phenylpent-4-ene-2,3-diol, necessary for the chemical synthesis of specific biologically active drugs such as daunomycin

Subcellular localization of Fad1p in Saccharomyces cerevisiae: a choice at post-transcriptional level?

FAD synthase is the last enzyme in the pathway that converts riboflavin into FAD. In Saccharomyces cerevisiae, the gene encoding for FAD synthase is FAD1, from which a sole protein product (Fad1p) is expected to be generated. In this work, we showed that a natural Fad1p exists in yeast mitochondria and that, in its recombinant form, the protein is able, per se, to both enter mitochondria and to be destined to cytosol. Thus, we propose that FAD1 generates two echoforms—that is, two identical proteins addressed to different subcellular compartments. To shed light on the mechanism underlying the subcellular destination of Fad1p, the 3′ region of FAD1 mRNA was analyzed by 3′RACE experiments, which revealed the existence of (at least) two FAD1 transcripts with different 3′UTRs, the short one being 128 bp and the long one being 759 bp. Bioinformatic analysis on these 3′UTRs allowed us to predict the existence of a cis-acting mitochondrial localization motif, present in both the transcripts and, presumably, involved in protein targeting based on the 3′UTR context. Here, we propose that the long FAD1 transcript might be responsible for the generation of mitochondrial Fad1p echoform

Chloroplast Omp85 proteins change orientation during evolution

The majority of outer membrane proteins (OMPs) from Gram-negative bacteria and many of mitochondria and chloroplasts are β-barrels. Insertion and assembly of these proteins are catalyzed by the Omp85 protein family in a seemingly conserved process. All members of this family exhibit a characteristic N-terminal polypeptide-transport–associated (POTRA) and a C-terminal 16-stranded β-barrel domain. In plants, two phylogenetically distinct and essential Omp85's exist in the chloroplast outer membrane, namely Toc75-III and Toc75-V. Whereas Toc75-V, similar to the mitochondrial Sam50, is thought to possess the original bacterial function, its homolog, Toc75-III, evolved to the pore-forming unit of the TOC translocon for preprotein import. In all current models of OMP biogenesis and preprotein translocation, a topology of Omp85 with the POTRA domain in the periplasm or intermembrane space is assumed. Using self-assembly GFP-based in vivo experiments and in situ topology studies by electron cryotomography, we show that the POTRA domains of both Toc75-III and Toc75-V are exposed to the cytoplasm. This unexpected finding explains many experimental observations and requires a reevaluation of current models of OMP biogenesis and TOC complex function