You mentioned serine integrase could be really beneficial for clinical applications (due to their shorter target cleavage site). Has it been tested in humans yet?
I don’t believe so. In fact, I don’t think either tyrosine or serine integrase have been used in any trials using humans – so far it’s been mostly just genetic modification in insects and small mammals.
Thank you! I’m gonna be honest – I am not confident on my ability to answer this. I believe that the letters themselves are arbitrary – they’re just assigned different letters to mark the different locations of the two complementary sites. It might actually stand for “left” and “right”? I am a bit unsure but great question!
Thank you! The only real shortcoming I can think of that serine integrase would face is that the specificity of serine’s targeting mechanism for recombination sites would make it somewhat difficult to manipulate in a lab setting, which possibly explains why researchers usually go for tyrosine in clinical trials.
So I just checked my research report again – because of how specific serine integrases can get with targeting an excision site, this sometimes works against them in the form of “pseudosites” – fake excision sites that pop up somewhere else in the DNA strand and proceed to confuse the hell out of the serine protein. This kind of mishap can sometimes result in damage to the DNA strand being split.
I am not sure on this, but it’s possible tyrosine integrases are simply more commonly found in phage genomes. From what I’ve seen on Phamerator, it looks like tyrosine may just be more prevalent as the integrase protein in phage genomes.
Thank you! There is one that comes immediately to mind. Tyrosine integrases are not as honed-in with their specificity when finding their excision site target in the DNA strand of choice – this means that tyrosine may be easier to manipulate than serine in a clinical/experimental setting.
curesymposium.org 
Great presentation! What reconnects the two split parts and recombines them?
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Thank you! The integrase proteins, which are a type of recombinase proteins, reconnect the split DNA from phage and bacteria into the prophage.
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You mentioned serine integrase could be really beneficial for clinical applications (due to their shorter target cleavage site). Has it been tested in humans yet?
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I don’t believe so. In fact, I don’t think either tyrosine or serine integrase have been used in any trials using humans – so far it’s been mostly just genetic modification in insects and small mammals.
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Great poster! I was just curious, what differentiates the attL and attR sites when recombination occurs?
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Thank you! I’m gonna be honest – I am not confident on my ability to answer this. I believe that the letters themselves are arbitrary – they’re just assigned different letters to mark the different locations of the two complementary sites. It might actually stand for “left” and “right”? I am a bit unsure but great question!
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I like the poster! Are there any short comings of serine integrase that you know of?
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Thank you! The only real shortcoming I can think of that serine integrase would face is that the specificity of serine’s targeting mechanism for recombination sites would make it somewhat difficult to manipulate in a lab setting, which possibly explains why researchers usually go for tyrosine in clinical trials.
LikeLike
So I just checked my research report again – because of how specific serine integrases can get with targeting an excision site, this sometimes works against them in the form of “pseudosites” – fake excision sites that pop up somewhere else in the DNA strand and proceed to confuse the hell out of the serine protein. This kind of mishap can sometimes result in damage to the DNA strand being split.
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what are the host provided proteins that trigger excision? More how big is the mechanism that has to catalyze that?
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Some of the accessory host proteins that tyrosine needs are the IHF protein and His protein.
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Do you have any predictions as to why tyrosine integrases are still so prevalent in clinical trials?
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I am not sure on this, but it’s possible tyrosine integrases are simply more commonly found in phage genomes. From what I’ve seen on Phamerator, it looks like tyrosine may just be more prevalent as the integrase protein in phage genomes.
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Hi, this was really interesting. I was wondering if there are any benefits to Tyrosine that could cause it to be used over Serine?
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Thank you! There is one that comes immediately to mind. Tyrosine integrases are not as honed-in with their specificity when finding their excision site target in the DNA strand of choice – this means that tyrosine may be easier to manipulate than serine in a clinical/experimental setting.
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