Research output: Contribution to journal › Article › peer-review
The genes of the sulphoquinovose catabolism in Escherichia coli are also associated with a previously unknown pathway of lactose degradation. / Kaznadzey, Anna; Shelyakin, Pavel; Belousova, Evgeniya et al.
In: Scientific Reports, Vol. 8, No. 1, 3177, 16.02.2018, p. 3177.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - The genes of the sulphoquinovose catabolism in Escherichia coli are also associated with a previously unknown pathway of lactose degradation
AU - Kaznadzey, Anna
AU - Shelyakin, Pavel
AU - Belousova, Evgeniya
AU - Eremina, Aleksandra
AU - Shvyreva, Uliana
AU - Bykova, Darya
AU - Emelianenko, Vera
AU - Korosteleva, Anastasiya
AU - Tutukina, Maria
AU - Gelfand, Mikhail S.
N1 - Publisher Copyright: © 2018 The Author(s).
PY - 2018/2/16
Y1 - 2018/2/16
N2 - Comparative genomics analysis of conserved gene cassettes demonstrated resemblance between a recently described cassette of genes involved in sulphoquinovose degradation in Escherichia coli K-12 MG1655 and a Bacilli cassette linked with lactose degradation. Six genes from both cassettes had similar functions related to carbohydrate metabolism, namely, hydrolase, aldolase, kinase, isomerase, transporter, and transcription factor. The Escherichia coli sulphoglycolysis cassette was thus predicted to be associated with lactose degradation. This prediction was confirmed experimentally: expression of genes coding for aldolase (yihT), isomerase (yihS), and kinase (yihV) was dramatically increased during growth on lactose. These genes were previously shown to be activated during growth on sulphoquinovose, so our observation may indicate multi-functional capabilities of the respective proteins. Transcription starts for yihT, yihV and yihW were mapped in silico, in vitro and in vivo. Out of three promoters for yihT, one was active only during growth on lactose. We further showed that switches in yihT transcription are controlled by YihW, a DeoR-family transcription factor in the Escherichia coli cassette. YihW acted as a carbon source-dependent dual regulator involved in sustaining the baseline growth in the absence of lac-operon, with function either complementary, or opposite to a global regulator of carbohydrate metabolism, cAMP-CRP.
AB - Comparative genomics analysis of conserved gene cassettes demonstrated resemblance between a recently described cassette of genes involved in sulphoquinovose degradation in Escherichia coli K-12 MG1655 and a Bacilli cassette linked with lactose degradation. Six genes from both cassettes had similar functions related to carbohydrate metabolism, namely, hydrolase, aldolase, kinase, isomerase, transporter, and transcription factor. The Escherichia coli sulphoglycolysis cassette was thus predicted to be associated with lactose degradation. This prediction was confirmed experimentally: expression of genes coding for aldolase (yihT), isomerase (yihS), and kinase (yihV) was dramatically increased during growth on lactose. These genes were previously shown to be activated during growth on sulphoquinovose, so our observation may indicate multi-functional capabilities of the respective proteins. Transcription starts for yihT, yihV and yihW were mapped in silico, in vitro and in vivo. Out of three promoters for yihT, one was active only during growth on lactose. We further showed that switches in yihT transcription are controlled by YihW, a DeoR-family transcription factor in the Escherichia coli cassette. YihW acted as a carbon source-dependent dual regulator involved in sustaining the baseline growth in the absence of lac-operon, with function either complementary, or opposite to a global regulator of carbohydrate metabolism, cAMP-CRP.
KW - ALPHA-SUBUNIT
KW - BACILLUS-SUBTILIS
KW - D-GALACTOSE METABOLISM
KW - FUNCTIONAL MODULES
KW - GENOME
KW - PROMOTER
KW - PROTEIN
KW - STAPHYLOCOCCUS-AUREUS
KW - SYSTEM
KW - TRANSCRIPTION ACTIVATION
UR - http://www.scopus.com/inward/record.url?scp=85042211653&partnerID=8YFLogxK
U2 - 10.1038/s41598-018-21534-3
DO - 10.1038/s41598-018-21534-3
M3 - Article
C2 - 29453395
AN - SCOPUS:85042211653
VL - 8
SP - 3177
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
IS - 1
M1 - 3177
ER -
ID: 12078882