Heredity

  • Deoxyribose has 5 carbon atoms, which are numbered clockwise

    • The 1’ (one prime) carbon holds the nitrogen base

    • The 3’ (three prime) carbon has a hydroxide that will bond with the P-group of another nucleotide

    • The 5’ (five prime) carbon holds onto the phosphate group

  • DNA is antiparallel because complementary strands run in opposite directions. Important because the 3’ and 5’ directions is how DNA is “read” by enzymes. 

  • HINT: The O on the deoxyribose sugar “points” to the 5’ end.

  • Pyrimidines (T, C, with single rings) always bond with purines (A, G, with double rings) in nucleic acids.

DNA bonds

  • Hydrogen bonds (weak attractions) hold bases together

    • T=A (2 bonds)

    • G=C (3 bonds)

  • Covalent phosphodiester bonds (strong bonds) hold nucleotides together at the backbone

  • DNA polymers: acid bases

  • Ligase: covalent bonds

    • Semi-conservative replications

  • Helicase: breaks hydrogen bonds, unwinds part of the DNA double helix,

  • Topoisomerase: untwist DNA, helps relieve the strain of unwinding by breaking, swiveling, and rejoining DNA strands

  • Primase: adds RNA primer so polymerase can attach

Protein Synthesis:

  • RNA

    • Ribose sugar

    • Uracil instead of thymine

    • Single stranded

    • Copies the information to take from the inside nucleus to the ribosome

      • mRNA (messenger): carries information from DNA to the ribosome

      • t:RNA (transfer):  carries amino acids to the ribosome

      • rRNA (ribosomal) : building blocks of ribosomes

      • microRNA (inhibit synthesis): small RNA molecules that bind to other RNA molecules to degrade them (more on these later)

    • The nucleotide sequence in the DNA is used to make a complementary sequence in mRNA

    • Uses many of the same enzymes from DNA replication - helicase, topoisomerase, RNA polymerase, etc.

    • RNA polymerase uses a single strand of DNA to make mRNA; works in the 5’ to 3’ direction

    • The DNA strand that is used is called the template strand, noncoding strand, minus strand, or antisense strand

  • Post-transactional Modification:

    • Before the mRNA leaves the nucleus - 

      • A poly-A tail is added (Protect the ends from degradation; like aglets on shoelaces)

      • A GTP cap is added

      • Splicing by spliceosomes

        • Introns stay in the nucleus; do not code for proteins

        • Exons exit the nucleus to go to the ribosome; do code for proteins

  • Translation:

    • Occurs at ribosomes

      • Free ribosomes in prokaryotes

      • Free ribosomes or bound ribosomes (to rough ER) in eukaryotes

    • In prokaryotes, translation occurs as the mRNA is being transcribed

    • In eukaryotes it occurs after transcription 

    • Three steps - initiation, elongation, and termination

      • Initiation

        • Small ribosomal subunit binds to mRNA and an initiator tRNA

        • Then the large ribosomal subunit attaches

      • Elongation

        • The ribosome moves down the mRNA in the 5’ to 3’ direction

        • For each codon (3 bases on the mRNA), a tRNA with a corresponding anticodon brings an amino acid to the ribosome

        • The amino acid is added to the preceding one by a peptide bond

      • Termination:

        • Elongation continues until the ribosome reaches a stop codon in the mRNA

          • UAG, UAA, or UGA

        • A protein called a release factor that causes the polypeptide chain to separate from the ribosome

  • Which amino acid gets added to the polypeptide?

    • Each codon in the mRNA corresponds to one amino acid

    • If the anticodon on the tRNA is complementary to the codon on the mRNA → the correct amino acid is at the ribosome and gets added

    • If the anticodon on the tRNA is not complementary to the codon on the mRNA → the correct amino acid is not at the ribosome; must wait for another tRNA with a complementary anticodon to arrive

    • The polypeptide folds up based on the arrangement of its amino acids (secondary and tertiary protein structure)

    • Some polypeptides combine with others to make larger proteins (quaternary structure)

    • May be packaged at ER or modified and p

      ackaged at the Golgi

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