Update on Degradosome
Function: The Importance of Location
By Mike Gene;
A few years ago, I used
some ID Thinking to come up with a testable hypothesis about the function of enolase (a glycolytic enzyme) as
part of the degradosome [1].
Enolase functions in the degradosome as a
prong that plugs the degradosome into the glycolytic pathway so that ATP generated by pyruvate kinase is then quickly
channeled to the helicase to fuel its unwinding
activity.
The logic was essentially
this:
ID
entails that these cellular processes are quite sophisticated. Consistent with
this prediction is a quasi-solid state cell, where order is paramount and
random processes are minimized. …… ID allows me to take a view of the cell more as a
sophisticated, machine-like entity rather than a jury-rigged hodgepodge cobbled
together by the Blind Watchmaker. This is because biomolecular
engineering at the hands of an advanced intelligence is likely to express its
intervention such that the products of design reflect a state that is elegantly
coherent. The expectation of a jury-rigged hodgepodge makes more sense in light
of non-teleological views, which begin with the random mess of the prebiotic soup and not the watch-type reality Paley once invoked.
So
I begin to think that the degradosome could indeed
reflect an originally designed state given its basic house-keeping role. If so,
what is enolase doing there? A non-teleological view gives me no reason to expect a logical reason
for it being there, as evolution doesn't have to be logical, in fact, it often
simply jury-rigs hodgepodge things together. But if enolase
was originally part of the degradosome, which in turn
was originally designed, I expect a logical
reason for it being there.
A paper has just recently
been published that, for the first time, demonstrates one of the possible roles
of enolase in degradosomal
function [2]. My prediction apparently
missed the bull’s eye, but not by too much.
Put simply, enolase function in the degradosome
is connected to glucose transport into the cell via glycolysis. It had been previously determined that if you
block glycolysis in its early stages, the mRNA for ptsG, which
encodes the major glucose transporter, is rapidly degraded. This makes sense, as a cell that cannot
efficiently metabolize glucose via glycolysis need
not transport it into the cell and instead turn to other fuel sources. Morita et al. [2] were able to show that if
you eliminate only the enolase component of the degradosome in a strain of bacteria where glycolysis is blocked, such that phosphosugars
begin to accumulate inside the cell, the mRNA for the glucose transporter is not degraded. Such degradation, in response to shutting
down glycolysis, depends on enolase
function.
But how does enolase function of the degradosome
actually interface with glucose transport?
Morita et. al suggest:
“one possible mechanism by which enolase
stimulates ptsG mRNA degradation would be to modulate
the membrane localization of RNase E.”
Thus, my ID thinking that
stresses location and order as important to function is supported. To get the degradosome
to degrade the glucose transporter mRNA, you have to bring the degradosome to the proper
area in an enolase-dependent manner. What’s more, the enolase
function of the degradosome does interfaces with
glucose transport, providing a connection
between glycolysis and degradosome
function. However, my original
specific hypothesis of enolase helping to shuttle
energy to the degradosome appears fatally wounded by
the fact that enolase/degradosome activity
target certain mRNA degradation only
when glycolysis is shut down.
There is much more to the degradosome story and the regulation of glucose transport
that in turn further underscores the theme of my prediction of “a quasi-solid
state cell, where order is paramount and random processes are minimized.” I will thus add to this essay in the future.
1. http://www.idthink.net/biot/degrad/index.html
2.
Morita, T., Kawamoto, H., Mizota, T., Inada,
T., and Aiba, H. 2004. Enolase
in the RNA degradosome plays a crucial role in the
rapid decay of glucose transporter mRNA in the response to phosphosugar
stress in E. coli. Mol. Micro. 54:
1063-1075.