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Applied and Environmental Microbiology, October 2006, p. 6743-6750, Vol. 72, No. 10
0099-2240/06/$08.00+0     doi:10.1128/AEM.00584-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Eukaryotic Lipid Body Proteins in Oleogenous Actinomycetes and Their Targeting to Intracellular Triacylglycerol Inclusions: Impact on Models of Lipid Body Biogenesis

Jan Hänisch,1,{dagger} Marc Wältermann,1,{dagger} Horst Robenek,2 and Alexander Steinbüchel1*

Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität, Corrensstrasse 3, D-48149 Münster,1 Department of Cell Biology and Ultrastructural Research, Leibniz Institute for Arteriosclerosis Research, University of Münster, D-48149 Münster, Germany2

Received 12 March 2006/ Accepted 15 July 2006

Bacterial neutral lipid inclusions are structurally related to eukaryotic lipid bodies. These lipid inclusions are composed of a matrix of triacylglycerols (TAGs) or wax esters surrounded by a monolayer of phospholipids. Whereas the monolayers of lipid bodies from animal and plant cells harbor specific classes of proteins which are involved in the structure of the inclusions and lipid homoestasis, no such proteins are known to be associated with bacterial lipid inclusions. The present study was undertaken to reveal whether the mammalian lipid body proteins perilipin A, adipose differentiation-related protein, and tail-interacting protein of 47 kDa (TIP47), which comprise the so called PAT family proteins, and the maize (Zea mays L.) oleosin are targeted to prokaryotic TAG bodies in vivo. When fused to enhanced green fluorescent protein, all proteins except the oleosin were mainly located at the surfaces of lipid inclusions when heterologously expressed in the recombinant actinomycetes Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155. A more detailed intracellular distribution analysis of TIP47 in recombinant R. opacus cells by immunocytochemical labeling of ultrathin cryosections and freeze fracture replicas revealed a substantial amount of TIP47 protein also pervading the cores of the inclusions. We discuss the impact of these results on the current model of lipid body biogenesis in prokaryotes.

* Corresponding author. Mailing address: Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität, Corrensstrasse 3, D-48149 Münster, Germany. Phone: 49 (251) 833 9821. Fax: 49 (251) 833 8388. E-mail: steinbu{at}uni-muenster.de.

{dagger} Jan Hänisch and Marc Wältermann contributed equally to this work.

Applied and Environmental Microbiology, October 2006, p. 6743-6750, Vol. 72, No. 10
0099-2240/06/$08.00+0     doi:10.1128/AEM.00584-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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