After sequencing a new genome for the first time, functional protein-coding genes are initially identified by: BLAST searches that look for viral integration in the host genome Bioinformatic searches that reveal consensus sequences in expressed genes Aligning expressed exons sequenced from cDNA using transcriptomics B and C A and BMany regions of non-coding eukaryotic DNA previously thought to be "junk" are now known to contain sequence elements important to regulating gene expression. What approach can be used to identify important non-coding regulatory regions when annotating a newly sequenced genome? comparing cDNA to genomic DNA to validate that the gene is expressed identifying restriction enzyme recognition sequences in the genome phylogenetic footprinting to identify conserved non-coding sequences searching for start/stop codons and splice recognition sites that predict where a gene might be locatedWhat feature of DNA replication did Fred Sanger cleverly take advantage of when he invented dideoxy DNA sequencing using ddNTPs? DNA polymerase requires helicase to open the template strands. Wobble rules allow occasional mispairing of bases. RNA nucleotides are degraded faster because they lack a 2' OH. Ligase creates a phosphodiester bond. DNA polymerase can only add new nucleotides to a 3' OH.Excellent! You've got your Wooly Mammoth hemoglobin growing up like crazy in E. coli. You purify the protein and start running some assays, and realize that your protein is not functional. You suspect that this may be because protein folding into tertiary and quaternary structure is highly temperature sensitive. Your E. coli love to grow at 37C (same temperature as their human hosts!), which may be way too warm for Wooly Mammoth hemoglobin to fold properly. You decide to team up with Dr. Esaki of Kyoto University to test their low-temperature protein expression system using the cold-adapted bacterium, Shewanella sp. (DOI: 10.1128/AEM.00824-07). That means you have to start over with your cloning, but… That's okay; you're just stoked to be doing international collaborative research That's okay; you're just stoked to be doing genetics and molecular biology (always your favorite subjects since college and your awesome Genetics professor!) You're bummed; you didn't realize that that's why research is called re-search, because you often have to re-do and re-peat everything Both A and BYou are considering using restriction enzymes that recognizes 4-bp and 6-bp nucleotide sequences, how often do you expect each enzyme to cut your 1,000 bp gene, respectively? 3 times and 1 time 4 times and 0 times 3 times and 0 times 4 times and 1 time 4 times and 3 timesGreat! Now you've got the Wooly Mammoth hemoglobin gene sequence with just the exons! You generate a restriction enzyme map of the region in and around your gene with the following restriction enzymes: T, H, E, N, A Which restriction enzymes do you choose to clone your DNA in the expression vector?T and HNETN and TWhy did you bother to identify the introns? So that I could include them in the sequence to understand intron function. So that I could exclude them from the sequence because prokaryotes don't have spliceosomal machinery. So that I could see how introns affect protein folding.Now you would like to clone it into an expression vector to grow up in a bacterial system. Because you're going to use bacteria to generate protein from a eukaryote, the mammoth, you need to get rid of introns from your sequence. How do you do that? Bioinformatically, I look for splice-site sequences and branch-point adenines and predict intron-exon boundaries I use a comparative genomic approach and use sequence homology with the genome of a closely related species I use a comparative genomic approach and use sequence homology with the genome of a distantly related species Both A and B Both B and CYou're the geneticist on a team that's uncovered a Wooly Mammoth in the ice and you want to study the function of its hemoglobin protein. First, you need to PCR amplify the gene to be able to Sanger sequence it. What reference genome do you use to design primers? The human genome because it's the best The bat genome because bats are cool The elephant genome because it likely has the most sequence similarity given evolutionary distance The E. coli genome because they're such a great model organism The yeast genome because they're small and they're a eukaryoteRecombinant DNA technology describes a set of molecular techniques that allow us to do what with specific DNA segments? Locate Isolate Alter Investigate All of the above

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Answered: Many regions of non-coding eukaryotic…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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After sequencing a new genome for the first time, functional protein-coding genes are initially identified by:

		BLAST searches that look for viral integration in the host genome
		Bioinformatic searches that reveal consensus sequences in expressed genes
		Aligning expressed exons sequenced from cDNA using transcriptomics
		B and C
		A and B

Many regions of non-coding eukaryotic DNA previously thought to be "junk" are now known to contain sequence elements important to regulating gene expression. What approach can be used to identify important non-coding regulatory regions when annotating a newly sequenced genome?

		comparing cDNA to genomic DNA to validate that the gene is expressed
		identifying restriction enzyme recognition sequences in the genome
		phylogenetic footprinting to identify conserved non-coding sequences
		searching for start/stop codons and splice recognition sites that predict where a gene might be located

What feature of DNA replication did Fred Sanger cleverly take advantage of when he invented dideoxy DNA sequencing using ddNTPs?

		DNA polymerase requires helicase to open the template strands.
		Wobble rules allow occasional mispairing of bases.
		RNA nucleotides are degraded faster because they lack a 2' OH.
		Ligase creates a phosphodiester bond.
		DNA polymerase can only add new nucleotides to a 3' OH.

Excellent! You've got your Wooly Mammoth hemoglobin growing up like crazy in E. coli. You purify the protein and start running some assays, and realize that your protein is not functional. You suspect that this may be because protein folding into tertiary and quaternary structure is highly temperature sensitive. Your E. coli love to grow at 37C (same temperature as their human hosts!), which may be way too warm for Wooly Mammoth hemoglobin to fold properly. You decide to team up with Dr. Esaki of Kyoto University to test their low-temperature protein expression system using the cold-adapted bacterium, Shewanella sp. (DOI: 10.1128/AEM.00824-07). That means you have to start over with your cloning, but…

		That's okay; you're just stoked to be doing international collaborative research
		That's okay; you're just stoked to be doing genetics and molecular biology (always your favorite subjects since college and your awesome Genetics professor!)
		You're bummed; you didn't realize that that's why research is called re-search, because you often have to re-do and re-peat everything
		Both A and B

You are considering using restriction enzymes that recognizes 4-bp and 6-bp nucleotide sequences, how often do you expect each enzyme to cut your 1,000 bp gene, respectively?

		3 times and 1 time
		4 times and 0 times
		3 times and 0 times
		4 times and 1 time
		4 times and 3 times

Great! Now you've got the Wooly Mammoth hemoglobin gene sequence with just the exons! You generate a restriction enzyme map of the region in and around your gene with the following restriction enzymes: T, H, E, N, A Which restriction enzymes do you choose to clone your DNA in the expression vector?

T and H

N and T

Why did you bother to identify the introns?

		So that I could include them in the sequence to understand intron function.
		So that I could exclude them from the sequence because prokaryotes don't have spliceosomal machinery.
		So that I could see how introns affect protein folding.

Now you would like to clone it into an expression vector to grow up in a bacterial system. Because you're going to use bacteria to generate protein from a eukaryote, the mammoth, you need to get rid of introns from your sequence. How do you do that?

		Bioinformatically, I look for splice-site sequences and branch-point adenines and predict intron-exon boundaries
		I use a comparative genomic approach and use sequence homology with the genome of a closely related species
		I use a comparative genomic approach and use sequence homology with the genome of a distantly related species
		Both A and B
		Both B and C

You're the geneticist on a team that's uncovered a Wooly Mammoth in the ice and you want to study the function of its hemoglobin protein. First, you need to PCR amplify the gene to be able to Sanger sequence it. What reference genome do you use to design primers?

		The human genome because it's the best
		The bat genome because bats are cool
		The elephant genome because it likely has the most sequence similarity given evolutionary distance
		The E. coli genome because they're such a great model organism
		The yeast genome because they're small and they're a eukaryote

Recombinant DNA technology describes a set of molecular techniques that allow us to do what with specific DNA segments?

		Locate
		Isolate
		Alter
		Investigate
		All of the above

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