10.1021/pr4003728.s002
Jieping Wang
Jieping
Wang
Han Mei
Han
Mei
Hongliang Qian
Hongliang
Qian
Qing Tang
Qing
Tang
Xiaocui Liu
Xiaocui
Liu
Ziniu Yu
Ziniu
Yu
Jin He
Jin
He
Expression Profile and Regulation
of Spore and Parasporal
Crystal Formation-Associated Genes in <i>Bacillus thuringiensis</i>
American Chemical Society
2013
Bacillus thuringiensisBacillus
CT
translational machineries
ribosome recycling
sporulation
parasporal crystals
translational machinery
spore
gene expression profiles
assembly
transcriptional regulation
insecticidal crystal proteins
Expression Profile
proteomics data
ω subunits
sigma factors
shock proteins
translational inhibition
ICP genes
pyruvate dehydrogenase
E 2 subunit
transcriptional factors
parasporal crystal formation
termination efficiency
mechanism
translation initiation
RNA polymerase
2013-12-06 00:00:00
Dataset
https://acs.figshare.com/articles/dataset/Expression_Profile_and_Regulation_of_Spore_and_Parasporal_Crystal_Formation_Associated_Genes_in_i_Bacillus_thuringiensis_i_/2346469
<i>Bacillus thuringiensis</i>, a Gram-positive endospore-forming
bacterium, is characterized by the formation of parasporal crystals
consisting of insecticidal crystal proteins (ICPs) during sporulation.
We reveal gene expression profiles and regulatory mechanisms associated
with spore and parasporal crystal formation based on transcriptomics
and proteomics data of <i>B</i>. <i>thuringiensis</i> strain CT-43. During sporulation, five ICP genes encoded by CT-43
were specifically transcribed; moreover, most of the spore structure-,
assembly-, and maturation-associated genes were specifically expressed
or significantly up-regulated, with significant characteristics of
temporal regulation. These findings suggest that it is essential for
the cell to maintain efficient operation of transcriptional and translational
machinery during sporulation. Our results indicate that the RNA polymerase
complex δ and ω subunits, cold shock proteins, sigma factors,
and transcriptional factors as well as the E2 subunit of the pyruvate
dehydrogenase complex could cooperatively participate in transcriptional
regulation via different mechanisms. In particular, differences in
processing and modification of ribosomal proteins, rRNA, and tRNA
combined with derepression of translational inhibition could boost
the rate of ribosome recycling and assembly as well as translation
initiation, elongation, and termination efficiency, thereby compensating
for the reduction in ribosomal levels. The efficient operation of
translational machineries and powerful protein-quality controlling
systems would thus ensure biosyntheses of a large quantity of proteins
with normal biological functions during sporulation.