Friday, 3 April 2015

The hunt for alkane degraders

As talked about in my previous post, bacterial degradation of alkanes is an important step in the bioremediation of crude oil from the environment. The key enzymes involved in the aerobic degradation of alkanes are the alkane hydroxylases (AHs), which hydroxylate alkanes to alcohols. The most commonly found AHs are the integral-membrane monooxygenases (AlkB) with a substrate  generally ranging from the n-alkanes C10 to C16. However, when fused with the rubredoxin protein, AlkB enzymes have been shown to hydrolyse n-alkanes up to C32. Another group of enzymes, which hydrolyse short and medium chain length alkanes, included in the AHs are the P450 CYP153. These enzymes are usually found in alkane degrading bacteria lacking alkB although they have also been found to coexist in some bacteria. Recent discoveries have found AH genes in new bacterial strains. This suggests the presence of further unknown alkane degrading bacteria and unknown AHs, which could be important to the degradation of n-alkanes in the natural environment and may have potential for industrial applications such as the bioremediation of crude oil. In order to investigate alkane degrading bacteria on a large scale, Nie et. al (2014) used microbial genome and metagonome data deposited in GenBank and the Integrated Microbial Genomes system.

2,069 complete and 1,910 draft microbial genomes representing 784 different genera (72 of which were Archaea) were used in this investigation. These were used to create a microbial proteomic database containing 15,399,030 protein sequences. In order to search for alkane hydroxylases in these genomes 28 alkB and 18 CYP153 characterised enzymes were used as references.  Along with the ‘best hits’ the authors also signified a hit in the protein sequence when there was a >40% similarity to CYP153 family members. Although P450 CYP153 enzymes may differ in their genome sequence to this extent, this seems to be a large value to use. This may vastly increase the likelihood of false positives, with protein sequences unable to degrade alkanes being categorised as alkane hydroxylase enzymes. Potential enzymes would therefore need to be tested for their ability to degrade alkanes to confirm results of this investigation. A similar process was also conducted to search for alkane hydroxylases in different metagenomes.

No archael genomes contained either alkB or CYP153 genes. Although the number of archaea genera used in this investigation were significantly lower than the amount of bacterial genera used, the lack of protein sequences matching these enzymes may suggest the degradation of alkanes by archaea uses a very different set of genes and enzymes. The authors did find 80 and 30 bacterial genera to contain alkB and CYP153 genes respectively. Some of these bacteria had previously not had proven alkane hydroxylation functions. Furthermore, their results suggested these are core genes in many genera and a vast amount were also novel genes. Similarly to archaea many Bacillus and Geobacillus genomes did not contain alkB or CYP153 genes although they have been shown to utilise long chain carbon sources and are found in many oil-related environments. This again suggests that alkB and CYP153 are not the key genes for alkane hydroxylation in these species.

Being able to understand the distribution of alkane hydroxylases in the environment is important to understand how crude oil will break down in different ecosystems. This could help planning the remediation of future oil spills such as by tailoring fertilisers to increase natural bioremediation or the addition of other bacteria to help clean up crude oil fractions which may be less utilised. The lack of alkane hydroxylases in some major groups indicates that some important genes involved in alkane degradation still remain elusive. More research will be able to shed more light on these processes. Bacteria and novel genes identified to hydrolyse alkanes in this study will also have to be tested in order to verify these findings.

Nie, Y., Chi, C. Q., Fang, H., Liang, J. L., Lu, S. L., Lai, G. L., ... & Wu, X. L. (2014). Diverse alkane hydroxylase genes in microorganisms and environments. Scientific reports4.

2 comments:

  1. Hi Ben, very interesting post. It would be very interesting to see what genes are responsible for alkane degradation in archeal communities and how they compare to the alkB and CYP153 genes.

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    1. Hi Maria, apart from saying they didn't contain these genes, the authors didn't discuss at all about archaeel alkane degradation. From what I've seen they may be more involved in anaerobic degradation which would obviously use different enzymes. It would be interesting to see how closely related alkane degradation enzymes are in archaea and bacteria though.

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