By R. K. Poole
Compliment for the Serial"This sequence has continuously offered a well-balanced account if development in microbial physiology...Invaluable for instructing purposes."- AMERICAN SCIENTISTAdvances in Microbial body structure used to be first released in 1967, and below the pioneering editorship of Professor Tony Rose, with the collaboration at quite a few occasions of John Wilkinson, Gareth Morris and Dave Tempest, the sequence has develop into immensely profitable and influential. The editors have continually striven to interpret microbial body structure within the broadest attainable context and feature by no means limited the contents to "traditional" perspectives of entire mobilephone physiology.Robert Poole was once appointed because the new editor following the premature demise of Tony Rose. less than Professor Poole's editorship, Advances in Microbial body structure keeps to submit topical and demanding stories, and to interpret body structure as commonly as long ago via together with all fabric that contributes to the certainty of the way microorganisms and their part components paintings. This remains to be the true problem of microbial body structure.
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Additional resources for Advances in Microbial Physiology, Vol. 37
While there is no compelling evidence for functional multi-enzyme cellulase complexes in aerobic fungi and bacteria, the cellulolytic Clostridium spp. produce tightly associated, extracellular cellulase complexes called cellulosomes. In C. , 1983a; Wiegel and Dykstra, 1984). Individual cellulosomes, isolated by elution of substrate with water, are discrete entities that are very resistant to dissociation and highly active on crystalline cellulose. Several strains of C. thermocellum have been investigated; all produce cellulosomes but these differ somewhat in size and organization.
Usually, the physical structure of the cellulosic substrate is not critical but unusual specificities are shown by the CBDs of XynD and CenC from C . , 1994). , 1988) and CBDs could be involved in targeting (see below). Deletion of the CBDs CELLULOSE HYDROLYSIS BY BACTERIA AND FUNGI 33 from T. , 1993) drastically reduced their affinities for xylan; other, related CBDs, from both xylanases and cellulases, have no apparent affinity for xylan, indicating that CBDs, even within families, may have different functional roles.
Sequence alignments are contained in Fujino et al. (1993). dPoly-(3-hydroxybutyrate) depolymerase. 'Exomaltopentaohydrolase. 'Chitinase. gExo-poly-a-D-galacturonosidase hAmylopullulanase 'Bifunctinal a-amylaselpullulanase. JPullulanase. kTranslated open reading frame. 'Outer membrane protein. 38 P. TOMME ET AL. domain and a carbohydrate-binding domain, so perhaps they function simply as spacer sequences or linkers (see below). , 1993). In this case, it can be argued that the Fn3 sequence acts as a linker and is required for the proper functioning of both domains on insoluble substrates.
Advances in Microbial Physiology, Vol. 37 by R. K. Poole