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Unraveling the Role of the rssC Gene of Serratia marcescens by Atomic Force Microscopy

Published online by Cambridge University Press:  20 October 2010

Bor-Ching Sheu*
Affiliation:
Department of Obstetrics and Gynecology, National Taiwan University, Taipei, 100-51, Taiwan
Chih-Chen Lin
Affiliation:
Department of Chemistry, Tamkang University, Tamsui, 251-37, Taiwan
Ying-Hsien Fu
Affiliation:
Department of Medical Biotechnology, Chang Gung University, Tao-Yuan, 333-02, Taiwan
Shih-Yuan Lee
Affiliation:
Department of Chemistry, Tamkang University, Tamsui, 251-37, Taiwan
Hsin-Chih Lai
Affiliation:
Department of Medical Biotechnology, Chang Gung University, Tao-Yuan, 333-02, Taiwan
Rung-Shin Wu
Affiliation:
Department of Chemistry, Tamkang University, Tamsui, 251-37, Taiwan
Chih-Hao Liu
Affiliation:
Institute of Applied Mechanics, National Taiwan University, Taipei, 106-17, Taiwan
Jui-Chang Tsai
Affiliation:
Centre for Optoelectronic Biomedicine, National Taiwan University, Taipei, 100-51, Taiwan
Shiming Lin*
Affiliation:
Institute of Applied Mechanics, National Taiwan University, Taipei, 106-17, Taiwan Centre for Optoelectronic Biomedicine, National Taiwan University, Taipei, 100-51, Taiwan
*
Corresponding author. E-mail: bcsheu@ntu.edu.tw
Corresponding author. E-mail: til@ntu.edu.tw
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Abstract

The product and direct role of the rssC gene of Serratia marcescens is unknown. For unraveling the role of the rssC gene, atomic force microscopy has been used to identify the surfaces of intact S. marcescens wild-type CH-1 cells and rssC mutant CH-1ΔC cells. The detailed surface topographies were directly visualized, and quantitative measurements of the physical properties of the membrane structures were provided. CH-1 and CH-1ΔC cells were observed before and after treatment with lysozyme, and their topography-related parameters, e.g., a valley-to-peak distance, mean height, surface roughness, and surface root-mean-square values, were defined and compared. The data obtained suggest that the cellular surface topography of mutant CH-1ΔC becomes rougher and more precipitous than that of wild-type CH-1 cells. Moreover, it was found that, compared with native wild-type CH-1, the cellular surface topography of lysozyme-treated CH-1 was not changed profoundly. The product of the rssC gene is thus predicted to be mainly responsible for fatty-acid biosynthesis of the S. marcescens outer membrane. This study represents the first direct observation of the structural changes in membranes of bacterial mutant cells and offers a new prospect for predicting gene expression in bacterial cells.

Type
Atomic Force Microscopy Biological Applications
Copyright
Copyright © Microscopy Society of America 2010

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References

REFERENCES

Binnig, G., Quate, C.F. & Gerber, C. (1986). Atomic force microscope. Phys Rev Lett 56, 930933.CrossRefGoogle ScholarPubMed
Camesano, T.A., Natan, M.J. & Logan, B.E. (2000). Observation of changes in bacterial cell morphology using tapping mode atomic force microscopy. Langmuir 16, 45634572.CrossRefGoogle Scholar
Chernov, K.G., Curmi, P.A., Hamon, L., Mechulam, A., Ovchinnikov, L.P. & Pastre, D. (2008). Atomic force microscopy reveals binding of mRNA to microtubules mediated by two major mRNP proteins YB-1 and PABP. FEBS Lett 582, 28752881.CrossRefGoogle ScholarPubMed
Cross, S.E., Kreth, J., Zhu, L., Sullivan, R., Shi, W.Y., Qi, F.X. & Gimzewski, J.K. (2007). Nanomechanical properties of glucans and associated cell-surface adhesion of Streptococcus mutans probed by atomic force microscopy under in situ conditions. Microbiology-Sgm 153, 31243132.CrossRefGoogle ScholarPubMed
Daschner, F.D. (1980). The epidemiology of Serratia marcescens. In The Genus Serratia, Graevenitz, A. & Rubin, S.J. (Eds.), pp. 187196. Boca Raton, FL: CRC Press.Google Scholar
Dupres, V., Alsteens, D., Pauwels, K. & Dufrene, Y.F. (2009). In vivo imaging of S-layer nanoarrays on Corynebacterium glutamicum. Langmuir 25, 96539655.CrossRefGoogle ScholarPubMed
Ehrenhofer, U., Rakowska, A., Schneider, S.W., Schwab, A. & Oberleithner, H. (1997). The atomic force microscope detects ATP-sensitive protein clusters in the plasma membrane of transformed MDCK cells. Cell Biol Int 21, 737746.CrossRefGoogle ScholarPubMed
Grimont, P.A.D. & Grimont, F. (1978). Genus Serratia. Ann Rev Microbiol 32, 221248.CrossRefGoogle ScholarPubMed
Ibrahim, K.S., Bakkiyaraj, D., James, R., Babu, T.G. & Pandian, S.T.K. (2009). Isolation and sequence analysis of a small cryptic plasmid pRK10 from a corrosion inhibitor degrading strain Serratia marcescens ACE2. Plasmid 62, 183190.CrossRefGoogle Scholar
Kloser, A., Laird, M., Deng, M. & Misra, R. (1998). Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12. Molec Microbiol 27, 10031008.CrossRefGoogle ScholarPubMed
Lai, H.C., Soo, P.C., Wei, J.R., Yi, W.C., Liaw, S.J., Horng, Y.T., Lin, S.M., Ho, S.W., Swift, S. & Williams, P. (2005). The RssAB two-component signal transduction system in Serratia marcescens regulates swarming motility and cell envelope architecture in response to exogenous saturated fatty acids. J Bacteriol 187, 34073414.CrossRefGoogle ScholarPubMed
Liu, J.H., Lai, M.J., Ang, S., Shu, J.W., Soo, P.C., Horng, Y.T., Yi, W.C., Lai, H.C., Luh, K.T., Ho, S.W. & Swift, S. (2000). Role of flhDC in the expression of the nuclease gene nucA, cell division and flagellar synthesis in Serratia marcescens. J Biomed Sci 7, 475483.Google ScholarPubMed
Matsuyama, T., Bhasin, A. & Harshey, R.M. (1995). Mutational analysis of flagellum-independent surface spreading of Serratia marcescens-274 on a low-agar medium. J Bacteriol 177, 987991.CrossRefGoogle ScholarPubMed
Matsuyama, T., Sogawa, M. & Nakagawa, Y. (1989). Fractal spreading growth of Serratia marcescens which produces surface-active exolipids. Fems Microbiol Lett 61, 243246.CrossRefGoogle Scholar
Matyka, K., Matyka, M., Mroz, I., Zalewska-Rejdak, J. & Ciszewski, A. (2007). An AFM study on mechanical properties of native and dimethyl suberimidate cross-linked pericardium tissue. J Mol Recognition 20(6), 524530.CrossRefGoogle Scholar
Mohanty, N. & Berry, V. (2008). Graphene-based single-bacterium resolution biodevice and DNA transistor: Interfacing graphene derivatives with nanoscale and microscale biocomponents. Nano Lett 8, 44694476.CrossRefGoogle ScholarPubMed
Neaves, K.J., Huppert, J.L., Henderson, R.M. & Edwardson, J.M. (2009). Direct visualization of G-quadruplexes in DNA using atomic force microscopy. Nucl Acids Res 37, 62696275.CrossRefGoogle ScholarPubMed
Olsen, J.D., Tucker, J.D., Timney, J.A., Qian, P., Vassilev, C. & Hunter, C.N. (2008). The organization of LH2 complexes in membranes from Rhodobacter sphaeroides. J Biol Chem 283, 3077230779.CrossRefGoogle ScholarPubMed
Raetz, C.R.H. & Whitfield, C. (2002). Lipopolysaccharide endotoxins. Ann Rev Biochem 71, 635700.CrossRefGoogle ScholarPubMed
Rock, C.O. & Jackowski, S. (2002). Forty years of bacterial fatty acid synthesis. Biochem Biophys Res Comm 292, 11551166.CrossRefGoogle ScholarPubMed
Soo, P.C., Horng, Y.T., Fu, Y.H., Lu, C.C. & Lai, H.C. (2008). A potential acyltransferase regulates swarming in Serratia marcescens. Biochem Biophys Res Comm 371, 462467.CrossRefGoogle ScholarPubMed
Wacker, D.A., Ruhl, D.D., Balagamwala, E.H., Hope, K.M., Zhang, T. & Kraus, W.L. (2007). The DNA binding and catalytic domains of poly(ADP-ribose) polymerase I cooperate in the regulation of chromatin structure and transcription. Mol Cell Biol 27, 74757485.CrossRefGoogle ScholarPubMed
Wang, J., Wan, Z., Liu, W., Li, L., Ren, L., Wang, X., Sun, P., Ren, L., Zhao, H., Tu, Q., Zhang, Z., Song, N. & Zhang, L. (2009). Atomic force microscope study of tumor cell membranes following treatment with anti-cancer drugs. Biosens Bioelectron 25, 721727.CrossRefGoogle ScholarPubMed