Editor: Aharon Oren
Structure and function of a cold shock domain fold protein, CspD, in Janthinobacterium sp. Ant5-2 from East Antarctica
Version of Record online: 18 APR 2011
© 2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved
FEMS Microbiology Letters
Volume 319, Issue 2, pages 106–114, June 2011
How to Cite
Mojib, N., Andersen, D. T. and Bej, A. K. (2011), Structure and function of a cold shock domain fold protein, CspD, in Janthinobacterium sp. Ant5-2 from East Antarctica. FEMS Microbiology Letters, 319: 106–114. doi: 10.1111/j.1574-6968.2011.02269.x
- Issue online: 17 MAY 2011
- Version of Record online: 18 APR 2011
- Accepted manuscript online: 22 MAR 2011 08:41AM EST
- Received 28 January 2011; revised 9 March 2011; accepted 11 March 2011., Final version published online 18 April 2011.
Fig. S1. Viable cell count of Ant5-2 after a single freeze–thaw cycle.
Fig. S2. Autoradiogram of 35S-methionine-labeled total cellular proteins from Ant5-2 cultures at different temperatures.
Fig. S3. Multiple sequence alignment of deduced amino acid sequence of the cold shock protein CspD from Ant5-2 with the cold shock transcriptional regulator sequence from J. lividum, CspE from H. arsenicoxydans, CspD1 from Janthinobacterium sp. Marseille, cold-shock DNA-binding protein family protein from T. denitrificans ATCC 25259, cold-shock DNA-binding protein family protein from D. aromatica RCB, CspD from B. phymatum STM815, CspA from N. meningitidis Z2491, cold shock protein from R. pickettii 12D and CspE from C. violaceum ATCC 12472.
Fig. S4. The agarose gel (1% w/v) showing the results of PCR amplification with CSPU5 and CSPU3 universal primers CSPU5 and CSPU3.
Fig. S5. SDS-polyacrylamide gel (12%, w/v) electrophoresis showing purified CspD of Ant5-2 expressed in Escherichia coli.
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