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Retired NBME 23 Answers

nbme23/Block 1/Question#16 (reveal difficulty score)
Physical analysis of the isolated genomic DNA ...
Methylase ๐Ÿ” / ๐Ÿ“บ / ๐ŸŒณ / ๐Ÿ“–
tags: biochem restriction_enzymes

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 +14  upvote downvote
submitted by โˆ—thomasalterman(181)
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Methylase methylates DNA, making the DNA resistant to restriction endonucleases

*https://d2jmvrsizmvf4x.cloudfront.net/7Pf4zZ3TuGwLTRKvUGYL_methylatedrestriction.jpg

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veryhungrycaterpillar  This is the best answer. +



 +13  upvote downvote
submitted by โˆ—imgdoc(183)
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Explanations for this are too complicated. Think of it like this:

You've got a piece of mutated DNA that is able to be digested by a restriction endonuclease, that means the DNA was transcriptionally available to begin with. AKA it was not methylated, because as we know, methylation = heterochromatin which is transcriptionally inactive. that means methylase was mutated

Only other plausible answer was DNase, and if it was mutated it would be inactive, not overactive.

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djeffs1  I mean sure... but this is a prokaryote... +



 +6  upvote downvote
submitted by โˆ—stinkysulfaeggs(125)
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Me reading this question stem: .....do you mean which of the following ENZYMES?

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 +6  upvote downvote
submitted by defalty98(5)
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Why are we complicating things? Change in the bases will destroy the palindromic sequence required for any restriction endonuclease to work. Methylation is the only option that makes sense.

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arcanumm  This makes sense have reading what your comment. I overlooked this and just assumed the GATC was a mutation that allowed the restriction enzyme to work on the mutant only. +2
arcanumm  it makes even more sense when looking at "numerous small fragments." Methylation is truly the obvious answer here in retrospect. +1
bgiri  DNAse can also cause a change in base by breaking down dna at the GATC sequence? +
almondbreeze  @bgiri Had the same reasoning - according to wiki, DNase catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. +



 +4  upvote downvote
submitted by pk33(6)
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In prokayotes Normally methylase adds methyl group to certain base(adenine) so restriction endonuclease can not recognize this site. If there is a mutation in methylase enzyme it can't add methyl group to adenine so restriction endonuclease can recognize it and can cleave it.

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 +0  upvote downvote
submitted by โˆ—carib_doc(0)
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My thought process for this one: In DNA mismatch repair for bacteria there is a parent strand and a newly synthesized strand. The parent strand is methylated prior to replication to allow it to be differentiated from the new strand in the case of mismatching. The new strand is identified by the lack of methylation and then degraded by endonucleases. So I used this logic to think altered methylase (decreased activity) allows for more DNA to be degraded by endonucleases. Not sure if its the best logic but it got me there lol

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 +0  upvote downvote
submitted by โˆ—an1(114)
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Resistant to digestion: does not break or get deactivated (endonuclease creates a nick in the strand, which means that it BREAKS the strand; even if it is for correction purposes) Deactivation is done by methylation; so if methylase is defective, the sequence will never be muted (digested/ broken down/ cleaved)

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an1  This could have also been written as deacetylation^^ +



 +0  upvote downvote
submitted by โˆ—consistentwrongdoer3(21)
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Why does methylation cause loss of resistance to GATC restriction endonuclease? Does this have to do with methylation of U to T?

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methylased  GATC related to methylase --> https://en.wikipedia.org/wiki/Dam_methylase +10
sympathetikey  Dam methylase, alright +2



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