INSPIRE is a new community resource for HEP literature and associated information. It is based on the combination of SPIRES content and features and the powerful Invenio software developed at CERN. The INSPIRE service will come online in fall of 2009, and be run by CERN, DESY, Fermilab and SLAC. Data preservation, to be successful, must not only preserve the data, but must also organize it and allow it to be found by those who would make use of it, and resources such as INSPIRE are ideally positioned and ready to provide this organization and context. In addition, INSPIRE will soon be ready to provide storage of smaller datasets, such as high-level analysis objects, as stand-alone objects placed in the repository or as objects associated with an analysis paper. This small project could pave the way towards the context and organization which is one piece of the infrastructure needed for all levels of data preservation.

Bacterialmicrocompartments (BMCs) are organelles composed entirely of protein. They promote specific metabolic processes by encapsulatingand colocalizing enzymes with their substrates and cofactors, by protecting vulnerable enzymes in a defined microenvironment, and bysequestering toxic or volatile intermediates. Prototypes of the BMCsare the carboxysomes of autotrophic bacteria. However, structures of similarpolyhedral shape are being discovered in an ever-increasing number of heterotrophic bacteria, where they participate in the utilization ofspecialty carbon and energy sources.Comparative genomics reveals that the potential for this type of compartmentalization is widespread acrossbacterial phyla and suggests that genetic modules encoding BMCs are frequently laterally transferred among bacteria. The diverse functionsof these BMCs suggest that they contribute to metabolic innovation in bacteria in a broad range of environments.

Cyanobacteria and some chemoautotrophic bacteria are able to grow in environments with limiting CO2 concentrations by employing a CO2-concentrating mechanism (CCM) that allows them to accumulate inorganic carbon in their cytoplasm to concentrations several orders of magnitude higher than that on the outside. The final step of this process takes place in polyhedral protein microcompartments known as carboxysomes, which contain the majority of the CO2-fixing enzyme, RubisCO. The efficiency of CO2 fixation by the sequestered RubisCO is enhanced by co-localization with a specialized carbonic anhydrase that catalyzes dehydration of the cytoplasmic bicarbonate and ensures saturation of RubisCO with its substrate, CO2. There are two genetically distinct carboxysome types that differ in their protein composition and in the carbonic anhydrase(s) they employ. Here we review the existing information concerning the genomics, structure and enzymology of these uniquely adapted carbonic anhydrases, which are of fundamental importance in the global carbon cycle.

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