Can introns still code for portion of protein?

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sundew773
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Can introns still code for portion of protein?

Post by sundew773 » Tue Jun 28, 2005 8:19 pm

My professor seems to think so. Though introns are spliced out of the mRNA, do they actually have the ability to influence portions of translated proteins?

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Post by MrMistery » Wed Jun 29, 2005 7:47 pm

No, they do not. you must have misunderstood. No professor in his right mind would say such a thing. Unless, of course he is conducting a research program on the subject :lol:
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Post by Jelanen » Thu Jun 30, 2005 1:25 am

Firstly, few college professors are in their right minds...its a job requirement. Second, introns can occasionally influence the translated protein. Splicing doesn't always work perfectly and sometimes splicing doesn't happen at all for a given intron, resulting in a different protein. Being an intron is relative to the translation..keeping an intron in might produce a similar protein that is also viable. BUT (always a big but), if splicing goes right and the excised sequence is truly an intron for the desired protein, then the intron is degraded by exonucleases pretty fast.

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Post by TuyetGiang » Thu Jun 30, 2005 8:59 am

I think everything has reason to exist ! So if intron exists, certainly it play a role in translation, as same as appendix in our bodies, we haven't found its functions. :P
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Post by chemistry_freako » Thu Jun 30, 2005 2:09 pm

Seems probable, especially if splicing or transcription doesn't go right - a slipback of one nucleotide (frameshift error) can give rise to an altogether different triplet, thus a different amino acid results, which affects the final protein which is translated from the mRNA. Then again, if there is absolute precision in the activity of the spliceosomes, i wouldn't be sure if introns will still end up getting translated to proteins =p

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Post by Poison » Thu Jun 30, 2005 3:34 pm

One of my stupid professors said that he believes it. And yes, he likes those subjects. By the way, no he is not a genetics proffessor. :)
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Post by MrMistery » Sat Jul 02, 2005 5:34 pm

Introns do not get translated... We know that for sure.. But think of it: bacteria don't have introns but eukaryotic cells do... So it has to be some form of evolution... We don't know their role yet, but then again, we don't know a lot of things
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Post by Poison » Sat Jul 02, 2005 6:45 pm

You wouldn't want to discuss this with my proffessor, Andrew. He always has something to say, relevant or irrelevant, doesn't matter for him. We all gave up discussing things because he was talking too much that we were tired. :lol: Or he has a final sentence: 'I am the teacher, you are the students!!!' I think you can guess how stupid he is. :)
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MrMistery
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Post by MrMistery » Sat Jul 02, 2005 8:00 pm

check my signature, ozge. And apply it...
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Post by Poison » Sun Jul 03, 2005 5:25 pm

Good signature, Andrew. Maybe also I can try UAA and UGA together with UAG. Saying it 3 times may be better. :D
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Post by MrMistery » Sun Jul 03, 2005 7:45 pm

If it gets him to stop it's worth it
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Post by chemistry_freako » Mon Jul 04, 2005 2:27 pm

lol =D
Hmm, a question just struck me -
when i was doing restriction digestion of pUC19 plasmid, using Sal I,
i got 2 bands on the agarose gel (agarose gel electrophoresis was subsequently carried out following the restriction),
but the problem is, there is only one restriction site on the plasmid (endonucleases are specific).
Therefore, was just wondering about a satisfactory explanation as to why there were 2 bands? =D
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