Exam 4 Flashcards
transcription
- process where RNA polymerase synthesizes one strand of RNA from a DNA template
- begins when DNA in a chromosome unwinds near gene to be transcribed
ribonucleotides
- assemble along the unwound DNA strand in a complementary sequence
- only one strand in a gene is transcribed
- but dif genes may be transcribed from dif strands
both eukaryotic and prokaryotic genes contain…
- transcriptional units made up of:
- promoter
- RNA-coding sequence(s)
- terminator region
promoter
- DNA sequence that the transcription apparatus recognizes and binds to
- located in the 5’UTR (upstream)
bacterial transcription
- many genes transcribed at once
- genes and proteins are almost always colinear
- 3 steps:
- initiation
- elongation
- termination
initiation of transcription
- first step in bacterial transcription
- RNApol binds to DNA at the gene’s promoter
- DNA helix unwinds
- RNA synthesis begins
elongation of transcription
- second step in bacterial transcription
- DNA threaded thru RNApol at transcription bubble
- RNA strand growing 5’ -> 3’
- A in DNA [paired with U in RNA
- 30-50 nucleotides per second
termination of transcription
- 3rd step in bacterial transcription
- RNApol reaches “bumps” in terminator region and falls off
polycistronic RNA
- in bacterial cells many genes can be transcribed at once
- RNA that codes form multiple proteins
genes and proteins are almost always ______ in bacteria
-colinear
eukaryotic transcription
- additional step to transcription after initiation, elongation, and termination
- final step= RNA processing
- step modifies newly synthesized RNA (heterogeneous nuclear RNA)
complex internal organization of eukaryotic genes
- promoter region
- introns (noncoding nucleotides that are transcribed but not translated into amino acid sequence of protein)
- exons (intervene between coding sequences)
RNA processiong
- final step of transcription of eukaryotic cells
- modifies heterogeneous nuclear RNA:
- caps added for initiation of translation and stability
- poly adenine tail (30-100 A’s long) added
- slicing removes introns
why transcription is a highly regulated process
- initiation of transcription (ex lac operon)
- splicing (alternative splicing yields dif proteins from same gene)
- nuclear export (mature mPNA hidden in nucleus and released w signals like first responders)
mutations to splice sights
- cause genetic disorders
- ex. beta-thalassemia inherited blood disorders
- improper splicing results in defective form of hemoglobin and anemia
translation of mRNA
- mRNA is translated from language of nucleic acids to amino acids (protein)
- enzymes and RNA translate mRNA
- euk: mature mRNA exported out of nucleus into cytoplasm to be translated by ribosomes
ribosomal RNA (rRNA)
-major component of ribosomes/ organelles that construct proteins
transfer RNA (tRNA)
- interpreters that read mRNA code and insert amino acids into growing protein
- cloverleaf structure
- amino acid attachment site at 3’ end (always CCA)
- each has unique anticodon which pairs to codon on mRNA during translation
- hydrogen bonds bwtn bases
flow of genetic info
- DNA is transcribed into RNA (genetic info is copied into mRNA)
- RNA is translated into protein (amino acids are polymerized into polypeptides which are then folded into proteins)
one gene, one-polypeptide hypothesis
-some proteins are composed of multiple polypeptides
proteins have variety of functions
- fibroin (spider’s web)
- luciferin (generates bioluminescence, firefly ex.)
- ricin (natural poison in castor beans)
3 characteristic groups of all (20) amino acid
- amino group (-NH2)
- carboxyl group (-COOH/ -COO)
- unique side chain (-R)
peptide bonds
-join amino acids to form polypeptide chains
polypeptides
- polar
- read from N-terminus to C-terminus
- after formation it folds into 3D shape (determined by a.a. sequence)
- once folded, polypeptide makes a protein
how is a proteins 3D shape determined
-protein’s amino acid sequence determines 3D structure and function
4 levels of protein structure
- primary
- secondary
- tertiary
- quaternary
primary level
- linear amino acid sequence in polypeptide chain
- most important level
secondary level
- hydrogen bonding btwn peptide bonds (backbone)
- causes amino acid to fold in pattern on itself
- forms 3D alpha helix fig, pleated flat sheet (or beta sheet), and randomized coil structures
- interactions btwn NH and CO groups
tertiary level
- folding of secondary structure back on itself again (side chain interactions)
- forms 3D folded polypeptide chain pattern
quaternary level
-interactions between two or more polypeptide chains