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11111nata11111 [884]
2 years ago
12

Which statements about the modification of chromatin structure in eukaryotes are true? Select all that apply. View Available Hin

t(s) Select all that apply. Deacetylation of histone tails in chromatin loosens the association between nucleosomes and DNA. Methylation of histone tails in chromatin can promote condensation of the chromatin. DNA is not transcribed when chromatin is packaged tightly in a condensed form. Acetylation of histone tails is a reversible process. Some forms of chromatin modification can be passed on to future generations of cells. Acetylation of histone tails in chromatin allows access to DNA for transcription.
Biology
1 answer:
Kay [80]2 years ago
7 0

The correct answers are:  

  • Methylation of histone tails in chromatin can promote condensation of the chromatin.
  • DNA is not transcribed when chromatin is packaged tightly in a condensed form.
  • Acetylation of histone tails is a reversible process.
  • Some forms of chromatin modification can be passed on to future generations of cells.  
  • Acetylation of histone tails in chromatin allows access to DNA for transcription.

Histone modifications are post-translational modifications of histone protein that can affect gene expression by altering chromatin structure or recruiting histone modifiers.The most common modifications are methylation, phosphorylation, acetylation and ubiquitylation. All of them affect the binding affinity between histones and DNA and thus loosening (gene activation) or tightening (gene repression) the condensed DNA.

Histone methylation is a transfer of methyl group by histone methyltransferases to lysine or arginine amino acid of protein. Effect of methylation depends on the type of protein that is modified. Demethylation is the reverse process.

Histone acetylation is the process of adding of an acetyl group(by  histone acetyltransferases) to histone proteins and it can also activate or inhibit the gene expression. Deacetilation is reverse process.

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A protein biochemist attempted to determine the amino acid sequence of a decapeptide. Use the results from the trypsin, chymotry
Maksim231197 [3]

Answer:

The possible sequence of the decapeptide is Met-Val-Lys-Tyr-Thr-Trp-Ala-Arg-Pro-Phe.

Explanation:

The cyanogen bromide cleaves the carboxyl end of Met (methionine and non-peptide). Trypsin cleaves on the C-terminal of Arg and Lys, however, not on the N-terminal of Pro, which signifies that Lys is the last amino acid in T2. Hence, Met-Val-Lys----. The middle part of the sequence can be predicted from the digestion done by chymotrypsin.

The chymotrypsin cleaves on the C terminal of Phe, Trp, Tyr, however, not on the N side of Pro. CT3 exhibit Lys, Met, Tyr, Val, as Met-Val and Tyr are the initial three amino acids, therefore, Tyr must be the fourth one. Now the sequence will be Met-Val-Lys-Tyr...

CT1 possesses Ala, Arg, Phe, Pro, as chymotrypsin cleaves the C side of the Phe, thus, the last amino acid should be Phe. Also, CT1 has Ala as the first amino acid. Also, trypsin does not cleave on the N-end of Pro. Thus, the sequence of CT1 strands will be Ala-Arg-Pro-Phe.  

In CT2, chymotrypsin cleaves on the C-side of trp. Thus, the sequence of CT2 strands as Thr-Trp is found in the middle. Thus, the whole sequence of the decapeptide strand will be:  

Met-Val-Lys-Tyr-Thr-Trp-Ala-Arg-Pro-Phe.  

3 0
3 years ago
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Answer:

Explanation:

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5 0
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