CBG.

05:

ara operon: Dual positive and

negative control

-
trp operon:

lac operon:

Zinc fingers
- one reason that proteins are so large is that they
must self-assemble inside cells
- our cell, on the other hand, often use a zinc atom
to take a short cut: by arranging 2 cys and 3 hys
close to each other in a chain, a protein can grab
a zinc ion and fold tightly around it
a short chain of 20-30 AA is enough to
create a solid, stable structure

- originally discovered in TFIII-A from frog eggs - the signal (after the transcription factors bind to
which contains 9 zinc fingers in a row; help the different sites in the enhancer DNA
stabilize the many copies of RNA as the cell sequence) is sensed using CREB-binding protein
develops or p300
- the string of zinc fingers curls along the DNA or a large domain in the centre acts as a
RNA strands, binding in the grooves and histone acetyltransferase, modifying histones in
extending AA inwards to read the bases nucleosomes and causing them to disassemble
- a single zinc finger does not bind very tightly and and reveal the gene;
can only recognize 2 or 3 bp, but when several
are strung together, the group binds more tightly
and can read longer DNA sequences
- the HIV-1 nucleocapsid protein contains 2 zinc
fingers that grip the viral RNA during budding of
the virus

Enhanceosome helps decide
the appropriate time to
transcribe a gene
- in order to specify which gene will be expressed
in a given situation, cells use a diverse collection
of DNA-binding proteins to control access to DNA
human genome encodes about 2,600
- when the cell is infected by viruses, several
different DNA-binding proteins are produced,
including ATF-s/c-Jun interferon response factor
(IRF) and nuclear factor kB (NF-kB); individually,
each one is not sufficient to activate the gene,
and each one also plays other roles in the
activation of other genes (NF-kB is also important
in immune responses, inflammation, apoptosis);
when they bind together, they activate the gene
and interferon is made
CREB-binding protein (blue) with domians from several
of its binding partners (green). Flexible portions not
seen in the structures are shown as dots
- assembly of the enhanceosome leads to removal
of the nucleosome, allowing the gene to be
expressed
- DNA bind to enhanceomers is nearly straight
- Interactions between the proteins is very limited,
even though the binding of the proteins is known
to be cooperative, such that binding of one
protein promotes the binding of others
proteins may promote binding by distorting
the DNA slightly into a preferred conformation
- Inside cells, CREB-binding protein or p300 might
generate a strong cooperative effect through its
binding to the different proteins