YiaC and CobB are enzymes that regulate lysine lactylation (Kla), a newly identified post-translational modification, in Escherichia coli. YiaC functions as a lysine lactylase to add lactyl groups to lysine residues, thereby increasing Kla levels. CobB serves as a lysine delactylase to remove lactyl groups from lysine and decrease Kla levels. Experiments showed that overexpressing YiaC increased Kla in E. coli, while overexpressing CobB decreased Kla. YiaC and CobB were also found to regulate Kla levels of various metabolic enzymes, and CobB could delactylate glycolysis enzymes in vitro.

1. Isabella Sofia González Berona
3er semester - Medicine UPB
01

2. 02
¿What is Escherichia Coli?
Member of the Enterobacteriacea, part of
the microbiota of the gastrointestinal tract.
Genetic elements or mutations that
determine the pathogenicity and virulence
different types of diseases.
Genome structure is highly flexible, mobility of
genetic material --> transposons, insertion
sequences, bacteriophages, and plasmids.

3. 03
¿What is YiaC and CobB?
YiaC: functions as a lysine
lactylase.
CobB: serves as a lysine
delactylase.
Lysine lactylation (Kla) was
recently reported as a newly
identified type of PTM.
CobB can delete PykF K382la
to enhance glycolysis and
promote E. coli growth.

4. Identify whether YiaC and CobB regulate lysine lactylation in Escherichia
coli.
Illustrate the molecular mechanism of Kla-mediated regulation of
glycolysis.
04
Objetives

5. Methods
05
Inmunoblot:
Separate proteins by electrophoresis,
detected with antibodies that recognize
the antigens on them. ¿it´s Kla in E. Coli?
Transformation:
The genetic alteration of a cell, and
incorporation, and expression of
exogenous genetic material.

6. 06
SDS-PAGE
Separate proteins according to their
electrophoretic mobility. Proteins are
denatured, losing their three-
dimensional conformation.
Methods
In vitro assay:
which the tissues studied remain within
the organism in which they are normally
found.in vitro experiments produce
exact results

7. 07
it was not clear if the Kla PTM existed in
prokaryotes -- Western Blot.
The regulatory enzymes of Kla to
understand their function and
regulatory mechanism in prokaryotes.
YiaC overexpression caused an
extensive and obvious increase in Kla
levels.
CobB overexpression decreased Kla
levels in E. coli, but CobB deficiency
increased Kla in E. coli.
Results

8. 08
YiaC catalyzed acetylation
but not succinylation
lactate could be effectively
converted to lactyl-CoA.
Results
YiaC and CobB can regulate the Kla
levels of diverse metabolic and
biosynthetic enzymes.
CobB can widely delactylate
glycolysis enzymes in vitro

9. 09
Zhang, D.- Li, L
Discussion
¨"Kla has an extensive regulatory
effect on metabolism in bacteria,
distinct from the regulatory
transcription of Kla in eukaryotes"
YES
“Changes in metabolism can mobilize
regulatory enzymes to regulate
acylation levels. Lactate accumulates
in E. coli under glucose fermentation”
YES
Olive, A. J
"Host microbial metabolites are a
critical factor influencing many
physiological processes and the
development of diseases".
YES
Liu, H.

10. 10
Conclussion
By understanding how
prokaryotes use lactate
as an important
metabolite in their
proliferation, it will allow
us to find better
treatments, based on
enzymatic regulation, of
the metabplites
mentioned in the article.
The regulation of enzymes
such as YiaC and CobB,
which have large
enzymatic functions, can
open doors in the field of
microbiology

11. 11
Conceptual maps