Streptomyces albidoflavus explained

Streptomyces albidoflavus is a bacterium species from the genus of Streptomyces which has been isolated from soil from Poland.[1] Streptomyces albidoflavus produces dibutyl phthalate and streptothricins.[2] [3]

Small noncoding RNA

See also: s-SodF RNA. Bacterial small RNAs are involved in post-transcriptional regulation. Using deep sequencing S. albidoflavus transcriptome was analysed at the end of exponential growth. 63 small RNAs were identified. Expression of 11 of them was confirmed by Northern blot. The sRNAs were shown to be only present in Streptomyces species.[4]

sRNA scr4677 (Streptomyces coelicolor sRNA 4677) is located in the intergenic region between anti-sigma factor SCO4677 gene and a putative regulatory protein gene SCO4676. scr4677 expression requires the SCO4677 activity and scr4677 sRNA itself seem to affect the levels of the SCO4676-associated transcripts.[5]

Targets of two of S. albidoflavus noncoding RNAs have been identified. Noncoding RNA of Glutamine Synthetase I was shown to modulate antibiotic production.[6] The small RNA scr5239 (Streptomyces coelicolor sRNA upstream of SCO5239) has two targets. It inhibits agarase DagA expression by direct base pairing to the dagA coding region, and it represses translation of methionine synthase metE (SCO0985) at the 5' end of its open reading frame.[7] [8]

Fatty acid synthesis

A crystal structure is available of the S. albidoflavus S-malonyltransferase. S. albidoflavuss ACP S-MT is involved in both fatty acid synthesis II and polyketide synthase and is structurally similar to Escherichia colis analogue.[9]

Usage in biotechnology

Strains of S. albidoflavus produce various antibiotics, including actinorhodin, methylenomycin, undecylprodigiosin,[10] and perimycin.[11] [12] Certain strains of S. albidoflavus can be used for heterologous protein expression.[13]

DNA repair

The Ku homolog is SCF55.25c. It contains a Shrimp alkaline phosphatase-like (SAP-like) domain at the C-terminus. S. albidoflavus produces a (putatively) single-domain protein SC9H11.09c which is homologous to the LigD NucDom which is common to many bacterial LigDs. (LigDs are a subfamily of DNA ligases. In bacteria many, but not all LigDs have additional nuclease domains branched from the universally present central ligase domain. If present - as in this case - the nuclease domain is an N-terminus extension.)[14]

Genetics

The genome consists of a single linear molecule, and although Ku would be expected to perform end maintenance, none has been observed so far.

See also

Further reading

External links

Notes and References

  1. 10.1134/S0003683813050025. Purification and characterization of Streptomyces albidoflavus antifungal components. Applied Biochemistry and Microbiology. 49. 5. 451. 2013. Swiontek Brzezinska. M.. Jankiewicz. U.. Burkowska. A.. 17097515.
  2. 10.1016/j.micres.2005.06.007. 16427514. Dibutyl phthalate, the bioactive compound produced by Streptomyces albidoflavus 321.2. Microbiological Research. 161. 2. 121–6. 2006. Roy. R.N.. Laskar. S.. Sen. S.K.. free.
  3. Book: Stuart Shapiro . Regulation of Secondary Metabolism in Actinomycetes . CRC Press . 1989 . 0-8493-6927-4 .
  4. Vockenhuber MP, Sharma CM, Statt MG, Schmidt D, Xu Z, Dietrich S, Liesegang H, Mathews DH, Suess B . 6 . Deep sequencing-based identification of small non-coding RNAs in Streptomyces coelicolor . RNA Biology . 8 . 3 . 468–77 . May 2011 . 21521948 . 3218513 . 10.4161/rna.8.3.14421 .
  5. Moody MJ, Jones SE, Elliot MA . Complex intra-operonic dynamics mediated by a small RNA in Streptomyces coelicolor . PLOS ONE . 9 . 1 . e85856 . 2014-01-01 . 24465751 . 3896431 . 10.1371/journal.pone.0085856 . 2014PLoSO...985856H . free .
  6. D'Alia D, Nieselt K, Steigele S, Müller J, Verburg I, Takano E . Noncoding RNA of glutamine synthetase I modulates antibiotic production in Streptomyces coelicolor A3(2) . Journal of Bacteriology . 192 . 4 . 1160–4 . February 2010 . 19966003 . 2812974 . 10.1128/JB.01374-09 .
  7. Vockenhuber MP, Suess B . Streptomyces coelicolor sRNA scr5239 inhibits agarase expression by direct base pairing to the dagA coding region . Microbiology . 158 . Pt 2 . 424–435 . February 2012 . 22075028 . 10.1099/mic.0.054205-0 .
  8. Vockenhuber MP, Heueis N, Suess B . Identification of metE as a second target of the sRNA scr5239 in Streptomyces coelicolor . PLOS ONE . 10 . 3 . e0120147 . 2015-01-01 . 25785836 . 4365011 . 10.1371/journal.pone.0120147 . 2015PLoSO..1020147V . free .
  9. White . Stephen W. . Zheng . Jie . Zhang . Yong-Mei . Rock . Charles O. . 2005 . The Structural Biology of Type II Fatty Acid Biosynthesis . . . 74 . 1 . 791–831 . 10.1146/annurev.biochem.74.082803.133524 . 0066-4154 . 15952903.
  10. Brian P, Riggle PJ, Santos RA, Champness WC . Global negative regulation of Streptomyces coelicolor antibiotic synthesis mediated by an absA-encoded putative signal transduction system . Journal of Bacteriology . 178 . 11 . 3221–31 . June 1996 . 8655502 . 178074 . 10.1128/jb.178.11.3221-3231.1996 .
  11. Liu CM, McDaniel LE, Schaffner CP . Fungimycin, biogenesis of its aromatic moiety . The Journal of Antibiotics . 25 . 3 . 187–8 . March 1972 . 5034814 . 10.7164/antibiotics.25.187 . free .
  12. Lee CH, Schaffner CP . Perimycin. The structure of some degradation products . Tetrahedron . 25 . 10 . 2229–32 . May 1969 . 5788396 . 10.1016/S0040-4020(01)82770-8 .
  13. Web site: Streptomyces coelicolor . John Innes Center . https://web.archive.org/web/20051019022921/http://www.jic.ac.uk/science/molmicro/Strept.html . dead . 19 October 2005 . 25 January 2010.
  14. Pitcher . Robert S. . Brissett . Nigel C. . Doherty . Aidan J. . Nonhomologous End-Joining in Bacteria: A Microbial Perspective . . . 61 . 1 . 2007 . 0066-4227 . 10.1146/annurev.micro.61.080706.093354 . 259–282. 17506672 .

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