The tryptophan operon

Unlike the lac operon that encodes catabolic enzymes, the

trp operon encodes anabolic enzymes
Enzymes for the biosynthesis of tryptophan: trpECDBA
Convert chorismic acid to tryptophan
Anthralinate synthase, indole-glycerol synthase,
tryptophan synthase
So when there is a lack of tryptophan, operon is ON
When there is an excess of tryptophan, operon is OFF

Strategy is opposite to that of the lac operon

Trp promoter and operator are overlapping
When tryptophan is low, aporepressor
cannot bind to operator and operon is
transcribed by RNA pol
When tryptophan is high, tryptophan binds to
the aporepressor, converting it into an active
repressor
Repressor binds to operator and blocks
binding of RNA pol

Tryptophan binding to TrpR

changes the shape of the protein

Attenuation adds an extra level of control on the trp operon

Because repression by trpR is relatively weak

RNA polymerase pauses &

falls off at the U-rich stretch
(rho-independent termination)

So how does low tryptophan overcome the attenuation?

Due to different secondary structures of the attenuator
More hydrogen
bonds and more
stable; has the
attenuator hairpin
Transcription is stopped

Fewer hydrogen
bonds and less
stable; lacks the
attenuator hairpin
Transcription continues

The leader senses tryptophan as it has 2 codons for

the amino acid
Dependent upon the fact that transcription and translation are coupled in bacteria

Presence of stalled ribosome

favours the less stable hairpin

Key factors for the trp-mediated

regulation of the attenuator
Transcription-translation are coupled
Ribosomes move at the same rate as RNA
polymerase
Even though some ribosomes are stalled at the
leader, translation initiation of each cistron can
occur independently
Other mechanisms: trp RNA-binding protein (TRAP) is bound
by tryptophan in B. subtilis; this binding activates TRAP which
binds the leader RNA and causes it to form a terminator
In E. coli the histidine operon has 7 histidine codons in a row!