Extremophiles, how to relate to their (?) proteins?

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In summary: The LipidsIn summary, the proteins in extremophile cells are different, and the adaptations to high temperature are also different.
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rwooduk
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We have briefly being introduced to extremophiles in class in our lectures on proteins and I'm struggling to relate the two.

For example say if you had an organism living in a high temperature environment what would be different about it's (?) proteins. Does that question even make sense? I'm trying to relate the two.

Thanks for any ideas.
 
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There are many adaptations that extremophiles have, this paper lists many of the differences in protein structure in a variety of extremophile types:

Protein[/PLAIN] [Broken] adaptations in Archaeal Extremophiles
Reed et al 2013
Archaea


Scroll down to section 2 where it covers thermophillic proteins. It goes into a lot of detail but the key features are:

Oligomerization and large hydrophobic core
Increased disulfide bond numbers
Increased salt-bridging
Increased surface charge
 
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  • #3
Ryan_m_b said:
There are many adaptations that extremophiles have, this paper lists many of the differences in protein structure in a variety of extremophile types:

Protein[/PLAIN] [Broken] adaptations in Archaeal Extremophiles
Reed et al 2013
Archaea


Scroll down to section 2 where it covers thermophillic proteins. It goes into a lot of detail but the key features are:

Oligomerization and large hydrophobic core
Increased disulfide bond numbers
Increased salt-bridging
Increased surface charge

Thats awesome thanks. So for my example, at high temperatures the protein would split apart (if my understanding of the word aggregate is correct), but for extremophiles that live in high temperature they have adapted so it doesnt.

very helpful thanks!
 
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If our understanding of Archaea is correct - they evolved before modern cells, likely at high temperatures. So protein structures in eukaryotic cells are a more recent adaptation.

But additional changes in the Archaea proteins has been ongoing as well. So that leaves a question - what were the proteins like in cyanobacteria and relatives before the Great Oxygenation Event?

http://en.wikipedia.org/wiki/Great_Oxygenation_Event
 
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jim mcnamara said:
If our understanding of Archaea is correct - they evolved before modern cells, likely at high temperatures.

The three major cell types evolved way before their modern (extant) members of course. But it is true that of them eukaryotes split last. [See "Evolution of the ribosome at atomic resolution", Petrov et al, PNAS, http://www.pnas.org/content/111/28/10251.full.pdf ; or the topologically equivalent usual 16S tree.]

Did Archaea evolve at high temperatures? Perhaps, but not necessarily.* It seems to be consensus that the universal common ancestry lineage bottlenecked through, or more likely rooted in, thermophilic cells.

Valentin's energy theory on Archaea, which is nicely consistent with Lane's energy theory on eukaryotes as high energy density specialists (due to coopting their mitochondria, likely and ironically originally ATP stealing parasites), is that Archaea evolved to be low energy density specialists. Perhaps it was the reason for the split, a population isolated by utilizing a scarce niche. That would predict their specialized low leakage membranes, makes chemiosmosis more efficient, a trait that can be coopted by archaean thermophilic extremophiles. As I understand it, but I can be mistaken, the high temperature limits are set by metabolic stress rather than inability to evolve functional cells. At sufficiently high temperatures cells can't grow so can't procreate, and at higher temperatures they starve to death.

*Depends on the dating of the split. If one peruses Timetree, one finds that Archaea and Bacteria split ~ 4 billion years ago.

That dating coincide with the late bombardment, which was a stochastic high temperature environment. According to models of Abramov et al, mesophiles would have survived too. But they could easily been among the many extinct lineages as thermophile lineages would be much more populous and so survive much more frequently. On the other hand, seeing Valentin's model, it looks more like a coincidence than a correlation, as scarce niches would have been abounding for all sorts of reasons.

But it is a molecular clock date, and to this layman those clocks seem to prefer to push their earliest splits as far back as they can. And there is very little other evidence that would test such deep dating.

The dating look reasonable, earliest oceans and likely continental crust has been evidenced in a zircon at ~ 4.40 billion years ago, and using Abramov et al models life could emerge at that time as the late veneer bombardment rapidly quenched after Moon formation ~4.47 billion years ago (recently rather securely dated with multiple methods, and the bombardment quenching too). And the first splits (here between Bacteria and Archaea) that we have surviving extant evidence of despite lineage extinction could happen a few hundred million years later. But is it valid, with all the uncertainty involved?

jim mcnamara said:
what were the proteins like in cyanobacteria and relatives before the Great Oxygenation Event?

Much the same I think, but evolved for anaerobic uses. Luckily modern OO protection stress enzymes seem to root in NO protection, and NOx would be produced at significant levels by volcanism in a CO2 atmosphere with ammonia among volcanic gases. So life survived its own global poisoning event.

Wouldn't we expect lipids to be more changed by evolution? Fish meat has the unfortunate trait to taste 'fishy' after prolonged increased oxygen environment, which I understand as an oxidation effect of fish oils. Et cetera.
 
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Trimethylamine is the "fishy smell" chemical you are referring to - see
http://en.wikipedia.org/wiki/Trimethylamine
Since it has an amine moiety it has to be derived from nitrogenous (proteins, polypeptides, amino acids) living -> dead material.
 
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What are extremophiles?

Extremophiles are organisms that thrive in extreme environmental conditions, such as high or low temperatures, high pressure, or high levels of acidity or alkalinity.

How do extremophiles relate to their proteins?

Extremophiles have unique proteins that are adapted to function in extreme environments. These proteins have different structures and properties compared to proteins found in non-extreme organisms.

Why do extremophiles produce unique proteins?

Extremophiles produce unique proteins in order to survive and thrive in extreme environments. These proteins are able to withstand the extreme conditions and maintain their function.

What are some examples of extremophiles and their unique proteins?

Some examples of extremophiles and their unique proteins include thermophiles, which produce heat-resistant proteins, and halophiles, which produce proteins that can withstand high levels of salt.

How do scientists study extremophiles and their proteins?

Scientists study extremophiles and their proteins through various methods, such as DNA sequencing, protein analysis, and biochemical and physiological experiments. They also use specialized equipment and techniques to simulate extreme environments in the lab.

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