Genetics DSM 13 & 14

AAUAAA put on 3' end to form mature mRNA

AUG followed by a number of codons and a stop codon in the same reading frame

DNA sequences where transcription regulatory proteins bind and are found on the same chromosome as the target they regulate

5' AUGCCC 3'

with similar sequences

frameshift mutations in bacteriophage T4

proteins that bind to DNA (cis-acting elements) and influence transcription

the number of reading frames

(NMP)n + NTP ---(rna pol)---> (NMP)n+1 + PPi (inorganic diphosphate)

transcription factor IID trans element

7-methylguanosine cap; stablizes

alternative splicing

where an exon moves in the genome to create a new gene

more than one codon in an mRNA. The third or wobble position in a codon has more flexible base-pairing, which allows a single anticodon on a tRNA to bind to more than one codon if the codon differs only in the third base. This wobble mechanism allows for the fidelity of translation when mutations occur in the third base of a codon.

the order of the codons in the mRNA determines the order of the amino acids in the encoded protein

The amino acid sequence of the coat protein from the bacteriophage MS2 corresponds to the order and sequence of the codons found in the gene.

RNA substitution editing and alternative exon splicing RNA substitution editing and alternative splicing are posttranscriptional modifications that can lead to a shorter protein. RNA substitution is a process in which a base is chemically modified to become a different base. If this new base introduces a stop codon in an mRNA, the resulting protein will be shorter. Alternative splicing is the process in which different combinations of exons are included in the final protein. If some exons are removed during alternative splicing, the final protein will be shorter.

The middle bases of a codon are similar for amino acids with similar chemical structures.

(3' of) the hairpin structure in the mRNA. Rho binds the rho utilization site (rut) as soon as it is transcribed at the 5' end of the mRNA. Rho moves towards the 3' end of the mRNA chasing the RNA polymerase. RNA polymerase is stalled by the hairpin structure at the 3' end of the mRNA, allowing rho to catch up. Rho dissociates the hairpin using helicase activity and dissociates the RNA polymerase after the hairpin structure.

a Tyr would be added to the protein when the ribosome reaches a UUG codon for Leu in an mRNA.

efficient re-use of ribosomes. In closed loop translation, the cap binding protein bound to the 5' end of the mRNA interacts with eIF4G, a protein that binds to the poly-A binding proteins at the 3' end of the mRNA, forming a loop with the mRNA. Ribosomes assemble at the cap of the mRNA near the 5' end of the molecule and dissociate after reaching the stop codon near the 3' end of the molecule. In closed loop translation, the 5' and 3' ends of the mRNA are near each other, which facilitates re-initiation of translation on the same molecule, a process called ribosome recycling.

Covalent linkage of an amino acid to the appropriate tRNA molecule.

ensures that equal amounts of each rRNA are made to be assembled into ribosomes.

An error in recombination such as crossing over at non-homologous sequences

ribozyme activity of the 23S rRNA.

radical group; 20 diff radical (R) groups that define 20 diff amino acids; R can be polar, non-polar, positively charged, and negatively charged

using protein fingerprinting to show a fragment of the mutant protein had different chemical properties.

covalent bond formed the carboxyl group of one amino acid and the amino group of another amino acid

Hydrogen bonds between the carboxyl groups and amino groups of different amino acids

a stably folded region of a protein. This region is usually associated with a specific function. Similar domains such as DNA binding domains can be found in diverse proteins that bind DNA. Many proteins have several different functional domains.

base pairing with the 16S rRNA in the small subunit of the ribosome.

The interface between the two ribosomal subunits is comprised mostly of RNA.

a release factor.

The location of transcription factors on the DNA does determine both where RNA polymerase II binds and the direction it moves along the DNA. However, the location of the transcription factors is initially determined by something else. In eukaryotes, binding of RNA polymerase II to DNA involves several other proteins known as transcription factors. Many of these transcription factors bind to the DNA in the promoter region (shown below in green), located at the 3' end of the sequence on the template strand. Although some transcription factors bind to both strands of the DNA, others bind specifically to only one of the strands.

a 5' GU splice junction and a 3' AG splice junction.

A longer than usual final transcript bc the intron could fail to be removed

-35 consensus Sigma subunit Prinbow box

enhancers RNA Polymerase II -30 TATA box

The sigma subunit helps RNA polymerase bind the promoter. This interaction is so strong that the RNA polymerase cannot leave the promoter. When the sigma subunit disassociates, this interaction is weakened, which allows the RNA polymerase to leave the promoter for elongation to begin.

three, one for each class of genes

repetition of the abbreviated bases

x^y (x = aas) (y = # of bases in codon)

a formyl group is attached to the initiating methionine

30S and 50S and they form 70S

tRNA in P site hydrogen bound to codon, another tRNA binds to Ef-TU and GTP in the A site and hydrogen binds to it's codon. the GTP is hydrolyzed to GDP and the Ef-TU GDP complex releases. ribozyme peptidyl transferase catalyzes peptide bond between the two aas. EF-G GTP binds to the ribosome, hydrolyzing the GTP and pulling the ribosome forward. once translocation has occurred (the A tRNA is now securely bonded in the P section), the E tRNA (formerly the P tRNA) is ejected (bc it is uncharged)

300

small subunit = A, P large subunit = A, P, E

small subunit binds to mRNA and to factors IF1, IF2, and IF3 (enhance stability of bond), as well as GTP, then the initiation complex f(ormyl)MET binds in the P SITE (the only binding that occurs first in the P site), causing IF3 to dissociate, and sets the reading frame. then, the large subunit binds to the mRNA, small subunit, intiation tRNA complex and the IF1 and IF2 dissociate

30

1 branch

2 branches

3 branches

1 = all -s 2 = all but 1 -s 3 = ... final = all +s

a = highest number of +s b = highest-1 number of +s c/final = least number of +s