Comparative morphology of the gas bladder in driftwood catfishes (Siluriformes: Auchenipteridae)

The gross morphology of the gas bladder is described and illustrated for representatives of most species and all valid genera of the Auchenipteridae (Siluriformes). Although, a simple cordiform gas bladder is present in some species of the family, others are characterized by their distinctive gas-bladder shape and diverticula disposition. An acute posterior end of the gas bladder characterizes Centromochlus heckelii and C. macracanthus, and is variably present in specimens of Auchenipterus. Tocantinsia piresi and Asterophysus batrachus have distinctive gas bladders differing in number of diverticula (two or many). The two species of Trachycorystes are diagnosed based on their gas bladder morphology: T. menezesi has a simple cordiform bladder, whereas T. trachycorystes has a pair of lateral diverticulum and, usually, a well-developed terminal diverticulum. Species of Auchenipterichthys are characterized by having a secondary bladder with simple chamber. Short or elongate and divergent terminal diverticula are exclusive to most cis-andine species of Trachelyopterus. Tetranematichthys and trans-andine species of Trachelyopterus share a well-developed secondary chamber or terminal diverticula ventrally or dorsally connected to the posterior chambers. The small-sized species of Ageneiosus have well-developed gas bladders with a pair of posterior diverticula, whereas large-sized species have a reduced gas bladder with tunica externa varying from non-, partially, or completely ossified. Eight phylogenetic characters are proposed based on the morphology of the gas bladder and associated structures in species of Auchenipteridae, and the evolution of those characters in the family discussed. J. Morphol., 2012. (C) 2012 Wiley Periodicals, Inc.

Insights into Phosphate Cooperativity and Influence of Substrate Modifications on Binding and Catalysis of Hexameric Purine Nucleoside Phosphorylases

The hexameric purine nucleoside phosphorylase from Bacillus subtilis (BsPNP233) displays great potential to produce nucleoside analogues in industry and can be exploited in the development of new anti-tumor gene therapies. In order to provide structural basis for enzyme and substrates rational optimization, aiming at those applications, the present work shows a thorough and detailed structural description of the binding mode of substrates and nucleoside analogues to the active site of the hexameric BsPNP233. Here we report the crystal structure of BsPNP233 in the apo form and in complex with 11 ligands, including clinically relevant compounds. The crystal structure of six ligands (adenine, 2'deoxyguanosine, aciclovir, ganciclovir, 8-bromoguanosine, 6-chloroguanosine) in complex with a hexameric PNP are presented for the first time. Our data showed that free bases adopt alternative conformations in the BsPNP233 active site and indicated that binding of the co-substrate (2'deoxy) ribose 1-phosphate might contribute for stabilizing the bases in a favorable orientation for catalysis. The BsPNP233-adenosine complex revealed that a hydrogen bond between the 5' hydroxyl group of adenosine and Arg(43*) side chain contributes for the ribosyl radical to adopt an unusual C3'-endo conformation. The structures with 6-chloroguanosine and 8-bromoguanosine pointed out that the Cl-6 and Br-8 substrate modifications seem to be detrimental for catalysis and can be explored in the design of inhibitors for hexameric PNPs from pathogens. Our data also corroborated the competitive inhibition mechanism of hexameric PNPs by tubercidin and suggested that the acyclic nucleoside ganciclovir is a better inhibitor for hexameric PNPs than aciclovir. Furthermore, comparative structural analyses indicated that the replacement of Ser(90) by a threonine in the B. cereus hexameric adenosine phosphorylase (Thr(91)) is responsible for the lack of negative cooperativity of phosphate binding in this enzyme.