- Functional analysis of Mpk1-mediated cell wall integrity signaling pathway in the thermotolerant methylotrophic yeast Hansenula polymorpha
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Hyunah Kim , Eun Jung Thak , Ji Yoon Yeon , Min Jeong Sohn , Jin Ho Choo , Jeong-Yoon Kim , Hyun Ah Kang
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J. Microbiol. 2018;56(1):72-82. Published online January 4, 2018
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DOI: https://doi.org/10.1007/s12275-018-7508-6
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Understanding the characteristics and regulation mechanisms
of cell wall integrity (CWI) in yeast is important not
only for basic research but also in biotechnological applications.
We found significantly different CWIs in two representative
strains of the thermotolerant methylotrophic yeast
Hansenula polymorpha. Compared to the A16 strain (classified
as Ogataea polymorpha), the DL1-L strain (classified as
Ogataea parapolymorpha) has a thinner cell wall that was
found to be more fragile following long-term cultivation and
more sensitive to zymolyase. To gain a deeper insight into this
difference, we compared the characteristics of the Mpk1pmediated
CWI signaling pathway in the two strains. While
a DL1-L mutant deficient in Mpk1p (mpk1Δ) showed severe
growth retardation at both normal and high growth temperatures
and in the presence of cell-wall disrupting agents, the
A16 mpk1Δ mutant displayed only a mild defect in cell growth.
Sorbitol effect on rescuing growth retardation was different
in the two mpk1Δ strains, which could partly be ascribed to
subtle differences in the activation of HOG pathway. Among
the cell wall disruptors evaluated, only caffeine clearly increased
phosphorylation of Mpk1p in DL1-L, but not in A16.
A transcriptome analysis of the DL1-L strain revealed that
caffeine significantly increased the expression of a subset of
cell-wall related genes in an Mpk1p-dependent manner, but
not the expected Rlm1-target genes. Taken together, our data
support an essential role for Mpk1p in maintaining CWI in
H. polymorpha, although the requirement for Mpk1p and
its regulation under diverse stress conditions varies depending
on the strain background.
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Citations
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Shaokai Li, Lixia Pan, Bin Zhang, Jie Bao
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Roghayeh Shirvani, Maryam Babaei, Motahare Baladi, Matthias G Steiger, Mohammad Barshan-tashnizi
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Frontiers in Microbiology.2018;[Epub] CrossRef
- Remodeling of the Glycosylation Pathway in the Methylotrophic Yeast Hansenula polymorpha to Produce Human Hybrid-Type N-Glycans
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Seon Ah Cheon , Hyunah Kim , Doo-Byoung Oh , Ohsuk Kwon , Hyun Ah Kang
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J. Microbiol. 2012;50(2):341-348. Published online April 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-2097-2
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763
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Abstract
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As a step forward to achieve the generation of human complex-
type N-glycans in the methylotrophic yeast Hansenula
polymorpha, we here report the modification of the yeast
glycosylation pathway by heterologous expression of the
human gene encoding β-1,2-N-acetylglucosaminyltransferase
I (GnTI). For the optimal expression of human GnTI in
the yeast Golgi compartment, the catalytic domain of the
GnTI was fused to various N-terminal leader sequences derived
from the yeast type II membrane proteins. The vectors
containing GnTI fusion constructs were introduced into
the H. polymorpha och1Δ single and och1Δalg3Δ double
mutant strains expressing the ER-targeted Aspergillus saitoi
α-1,2 mannosidase, respectively. Both of the glycoengineered
Hpoch1Δ and Hpoch1ΔHpalg3Δ strains were shown to produce
successfully the hybrid-type glycans with a monoantennary
N-acetylglucosamine (GlcNAc1Man5GlcNAc2 and
GlcNAc1Man3GlcNAc2, respectively) by N-glycan profile
analysis of cell wall proteins. Furthermore, by comparative
analysis of byproduct formation and the glycosylation site
occupancy, we propose that the Hpoch1Δ strain would be
more suitable than the Hpoch1ΔHpalg3Δ strain as a host
for the production of recombinant proteins with humanized
glycans.
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