Mayer, F.: Principles of functional and structural organization in the bacteria cell: „Compartments“ and their enzymes. FEMS Microbiol. Rev. 104, 327-346 (1993)

Mayer, F.: Cell Structure. In: Rehm, H.-J., Reed, G. (Hrsg.), Biotechnology, Second edit., Vol. 1, pp. 5-46. VCH Verlagsgesellschaft, Weinheim, 1993

Mayer, F.: „Compartments“ in the bacterial cell and their enzymes. ASM News 59, 346-350 (1993)

Hoppert, M., Mayer, F.: Structural aspects of the interaction between phycobilisomes and thylakoid membranes in the unicellular cyanobacterium Synechococcus leopoliensis. Plant Physiol. (Life Sci. Adv.) 14, 11-19 (1995)

Liu, S.Y., Rainey, F.A., Morgan, H.W., Mayer, F., Wiegel, J.: Thermoanaerobacterium aotearoense sp. nov., a slightly acidophilic, anaerobic thermophile isolated from various hot springs in New Zealand, and emendation of the genus Thermoanaerobacterium. Int. J. Syst. Bacteriol. 46 (2), 388-396 (1996)

Engle, M., Li, Y., Rainey, F., Deblois, S., Mai, V., Reichert, A., Mayer, F., Messner, P., Wiegel, J.: Thermobrachium celere, gen. nov., sp. nov., a rapidly growing thermophilic, alkalitolerant, and proteolytic obligate anaerobe. Int. J. Syst. Bacteriol. 46, 1025-1033 (1996)

Gonzalez, J.M., Mayer, F., Moran, M.A., Hodson, R.E., Whitman, W.B.: Microbulbifer hydrolyticus gen. nov., sp. nov., and Marinobacterium georgiense gen. nov., sp. nov., two marine bacteria from a lignin-rich pulp mill waste enrichment community. Int. J. Syst. Bacteriol. 47, 369-376 (1997)

Slobodkin, A., Reysenbach, A.-L., Strutz, N., Dreier, M., Wiegel, J.: Thermoterrabacterium ferrireducens gen. nov., sp. nov., a thermophilic anaerobic dissimilatory Fe(III)-reducing bacterium from a continental hot spring. Int. J. Syst. Bacteriol. 47, 541-547 (1997)

Figures:

• Cell of Escherichia coli with two flagella and numerous fimbriae (typeI pili). Metal shadowing
• Dividing cell of Methanogenium marisnigri prepared by freeze-etching. Note the surface layer (S layer) and

several flagella.
• Methanococcus jannaschii, an extremely thermophilic methanogen from a submarine hydrothermal vent.
• Thermoterrabacterium ferrireducens, a thermophilic anaerobic dissimilatory Fe(III)-reducing bacterium from a

continental hot spring. Growth was on basal medium with amorphous Fe(III) oxide as an electron acceptor. The
cells are covered by a layer of very electron-dense particulate material. Ultrathin section.
• Structure of the flagellum of Acetobacterium woodii (inset: negatively stained flagellar basal body removed from the cell)
• Polyhydroxyalkanoic acid (PHA) synthase at the surface of the boundary layer of PHA inclusion bodies from Chromatium vinosum.
• Ultrastructural organization of the boundary layer of a PHA inclusion body from Pseudomonas oleovorans. Negative staining.

Liebergesell, M., Mayer, F., Steinbüchel, A.: Analysis of polyhydroxyalkanoic acid-biosynthesis genes of anoxygenic phototrophic bacteria reveals synthesis of a polyester exhibiting an unusual composition. Appl. Microbiol. Biotechnol. 40, 292-300 (1993)

Pieper-Fürst, U., Madkour, M.H., Mayer, F., Steinbüchel, A.: Purification and characterization of a 14-kDa protein that is bound to the surface of polyhydroxyalkanoic acid granules in Rhodococcus ruber. J. Bacteriol. 176, 4328-4337 (1994)

Liebergesell, M., Sonomoto, K., Madkour, M., Mayer, F., Steinbüchel, A.: Purification and characterization of the polyhydroxyalkanoic acid (PHA) synthase from Chromatium vinosum and localization of the enzyme at the surface of PHA granules. Eur. J. Biochem. 226, 71-80 (1994)

Wieczorek, R., Pries, A., Steinbüchel, A., Mayer, F.: Analysis of a 24-kDa protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus. J. Bacteriol. 177, 2425-2435 (1995)

Pieper-Fürst, U., Madkour, M.H., Mayer, F., Steinbüchel, A.: Identification of the region of a 14-kilodalton protein of Rhodococcus ruber that is responsible for the binding of this Phasin to polyhydroxyalkanoic acid granules. J. Bacteriol. 177, 2513-2523 (1995)

Steinbüchel, A., Aerts, K., Babel, W., Föllner, C., Liebergesell, M., Madkour, M.H., Mayer, F., Pieper-Fürst, U., Pries, A., Valentin, H.E., Wieczorek, R.: Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions. Can. J. Microbiol. 41, Suppl. 1, 94-105 (1995)

Alvarez, H.M., Mayer, F., Fabritius, D., Steinbüchel, A.: Formation of intracytoplasmic lipid inclusions by Rhodococcus opacus strain PD630. Arch. Microbiol. 165, 377-386 (1996)
 

Mayer, F., Hoppert, M.: Determination of the thickness of the boundary layer surrounding bacterial PHA inclusion bodies, and implications for models describing the molecular architecture of this layer. J. Basic Microbiol. 37, 45-52 (1997)

Föllner, C.G., Madkour, M., Mayer, F., Babel, W., Steinbüchel, A.: Analysis of PHA granule-associated proteins GA20 and GA11 in Methylobacterium extorquens and Methylobacterium rhodesianum. J. Basic Microbiol. 37, 11-21 (1997)

Mayer, F., Madkour, M.H., Pieper-Fürst, U., Wieczorek, R., Liebergesell, M., Steinbüchel, A.: Electron microscopic observations on the macromolecular organization of the boundary layer of bacterial PHA inclusion bodies. J. Gen. Appl. Microbiol. 42, 445-455 (1996)

 

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Gerberding, H., Mayer, F.: Interaction and compartmentalization of the components of bacterial enzyme systems involved in cell energetics. Z. Naturforsch. 48c, 535-541 (1993)

Specka, U., Mayer, F.: Cellular location, activity states, and macromolecular organization of glycoamylase in Clostridium thermosaccharolyticum. Arch. Microbiol. 160, 284-287 (1993)

Stupperich, E., Juza, A., Hoppert, M., Mayer, F.: Cloning, sequencing and immunological characterization of the corrinoid-containing N5-methyltetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 217, 115-121 (1993)

Kricke, J., Varma, A., Miller, D., Mayer, F.: Carboxymethyl cellulase from Bacillus sp.: isolation, macromolecular organization, and cellular location. J. Gen. Appl. Microbiol. 40, 53-62 (1994)

Reidlinger, J., Mayer, F., Müller, V.: The molecular structure of the Na+-translocating F1F0-ATPase of Acetobacterium woodii as revealed by electron microscopy resembles that of H+-translocating ATPases. FEBS Lett. 356, 17-20 (1994)

Braks, I., Hoppert, M., Roge, S., Mayer, F.: Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg. J. Bacteriol. 176, 7677-7687 (1994)

Birkenhäger, R., Hoppert, M., Deckers-Hebestreit, G., Mayer, F., Altendorf, K.H.: The F0 complex of the ATP synthase of Escherichia coli: Investigation by electron spectroscopic imaging and immunoelectron microscopy. Eur. J. Biochem. 230, 58-67 (1995)

Kolmar, H., Hennecke, F., Götze, K., Janzer, B., Vogt, B., Mayer, F., Fritz, H.-J.: Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J. 14, 3895-3904 (1995)

Friedebold, J., Mayer, F., Bill, E., Trautwein, A.X., Bowien, B.: Structural and immunological studies on the soluble formate dehydrogenase from Alcaligenes eutrophus. Biol. Chem. Hoppe-Seyler 376, 561-568 (1995)

Eismann, K., Mlejnek, K., Zipprich, D., Hoppert, M., Gerberding, H., Mayer, F.: Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm. J. Bacteriol. 177, 6309-6312 (1995)

Wilms, R., Freiberg, C., Wegerle, E., Meier, I., Mayer, F., Müller, V.: Subunit structure and organization of the genes of the A1A0 ATPase from the archaeon Methanosarcina mazei Gö1. J. Biol. Chem. 271, 18843-18852 (1996)
 

Figures:

• Macromolecular organization of the cytoplasmic enzyme complex D-ribulose-1,5-bisphosphate

carboxylase/oxygenase from Ralstonia eutropha (formerly Alcaligenes eutrophus).
• The cellulolytic enzyme system of Clostridium thermocellum as revealed by electron microscopy of negatively

stained samples.
• Immunoelectron microscopic localization of the membrane-bound hydrogenase in Ralstonia eutropha (formerly

Alcaligenes eutrophus) as revealed by the whole-mount immuno technique combined with negative staining.
• The methanoreductosome in methanogenic archaea.

Hoppert, M., Braks, I., Mayer, F.: Stability and activity of hydrogenases of Methanobacterium thermoautotrophicum and Alcaligenes eutrophus in reversed micellar systems. FEMS Microbiol. Lett. 118, 249-254 (1994)

Mayer, F., Hoppert, M.: Functional compartmentalization in Bacteria and Archaea: A hypothetical interface between cytoplasmic membrane and cytoplasm. Naturwiss. 83, 36-39 (1996)

Hoppert, M., Mlejnek, K., Seiffert, B., Mayer, F.: Activities of microorganisms and enzymes in water-restricted environments: Biological activities in aqueous compartments at µm-scale. In: Hoover, B. (ed.) Instruments, Methods, and Missions for the investigation of extraterrestrial microorganisms, SPIE Proceedings Series, Vol. 3111, pp. 501-509, 1997

Figure: The cartoon of an enzyme entrapped inside a reversed micelle (A) and bound to a membrane (B) illustrates the similarity between the two situations.  

 

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Hoppert, M., Mayer, F.: Electron microscopic technique for immunocytochemical localization of enzymes in methanogenic archaea. In: Archaea. A laboratory manual (Robb, F.T., Place, A.R., Sowers, K.R., Schreier, H.J., DasSarma, S., Fleischmann, E.M., eds.), pp. 269-278, Cold Spring Harbor Laboratory Press, 1995

Vogt, B., Berker, R., Mayer, F.: Improved contrast by a simplified post-staining procedure for ultrathin sections of resin-embedded bacterial cells: application of ruthenium red. J. Basic Microbiol. 35, 349-355 (1995)
 

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Books

Mayer, F.: Cytology and morphogenesis of bacteria (Volume of Handbook of Plant Anatomy). Gebrüder Bornträger, Berlin, Stuttgart (1986)

Robinson, D.G., Ehlers, U., Herken, R., Herrmann, B., Mayer, F., Schürmann, F.-W.: Methods of preparation for electron microscopy - an introduction for the biomedical sciences. Springer, Berlin, Heidelberg, New York (1987)

Mayer, F. (ed.): Methods in Microbiology, Vol. 20: Electron Microscopy in Microbiology. Academic Press, London (1988)

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