INVESTIGADORES
MORENO Silvia Margarita
artículos
Título:
Mucor rouxii Rho1 protein; characterization and possible role in polarized growth
Autor/es:
ARGIMÓN, S., GALELLO, F., PEREYRA, E., ROSSI, S. AND MORENO, S.
Revista:
ANTON LEEUW INT. J. G.
Referencias:
Año: 2007 vol. 91 p. 237 - 251
ISSN:
0003-6072
Resumen:
Abstract We have previously shown that protein
kinase A of the medically important zygomyceteWe have previously shown that protein
kinase A of the medically important zygomycete
Mucor rouxii participates in fungal morphology
through cytoskeletal organization. As a first step
towards finding the link between protein kinase A
and cytoskeletal organization we here demonstrate
the cloning of the RHO1 gene and the
characterization of its protein product. The Rho1
protein primary sequence shows 7085% identity
with fungal RHO1 or mammalian RhoA. Two
protein kinase A phosphorylation sequences in
adequate context are predicted, Ser73 and Ser135.
The peptide IRRNSQKFV, containing Ser135
proved to be a good substrate for M. rouxii protein
kinase A catalytic subunit. The over-expressed
Rho1 fully complements a Saccharomyces cerevisiaeparticipates in fungal morphology
through cytoskeletal organization. As a first step
towards finding the link between protein kinase A
and cytoskeletal organization we here demonstrate
the cloning of the RHO1 gene and the
characterization of its protein product. The Rho1
protein primary sequence shows 7085% identity
with fungal RHO1 or mammalian RhoA. Two
protein kinase A phosphorylation sequences in
adequate context are predicted, Ser73 and Ser135.
The peptide IRRNSQKFV, containing Ser135
proved to be a good substrate for M. rouxii protein
kinase A catalytic subunit. The over-expressed
Rho1 fully complements a Saccharomyces cerevisiaeRHO1 gene and the
characterization of its protein product. The Rho1
protein primary sequence shows 7085% identity
with fungal RHO1 or mammalian RhoA. Two
protein kinase A phosphorylation sequences in
adequate context are predicted, Ser73 and Ser135.
The peptide IRRNSQKFV, containing Ser135
proved to be a good substrate for M. rouxii protein
kinase A catalytic subunit. The over-expressed
Rho1 fully complements a Saccharomyces cerevisiaeRHO1 or mammalian RhoA. Two
protein kinase A phosphorylation sequences in
adequate context are predicted, Ser73 and Ser135.
The peptide IRRNSQKFV, containing Ser135
proved to be a good substrate for M. rouxii protein
kinase A catalytic subunit. The over-expressed
Rho1 fully complements a Saccharomyces cerevisiaeM. rouxii protein
kinase A catalytic subunit. The over-expressed
Rho1 fully complements a Saccharomyces cerevisiaeSaccharomyces cerevisiae
null mutant. The endogenous protein was
identified by western blot against a developed
antibody and by ADP-ribosylation. Localization
in germlings was visualized by immunofluorescence;
the protein was localized in patches in the
mother cell surface and excluded from the germ
tube. Measurement of Rho1 expression during
germination indicates that Rho1, at both the
mRNA and protein levels, correlates with differentiation
and not with growth. Rho1 has been
shown to be the regulatory protein of the b-1,3-
glucan synthase complex in fungi in which b-1,3-
glucans are major components of the cell wall.
Even though glucans have not been detected in
zygomycetes, caspofungin, an echinochandin
known to be an inhibitor of b-1,3-glucan synthase
complex, is shown here to have a negative effect
on growth and to produce an alteration on morphology
when added to M. rouxii growth culture
medium. This result has an important impact on
the possible participation of b-1,3-glucans on the
regulation of morphology of zygomycetes.b-1,3-
glucan synthase complex in fungi in which b-1,3-
glucans are major components of the cell wall.
Even though glucans have not been detected in
zygomycetes, caspofungin, an echinochandin
known to be an inhibitor of b-1,3-glucan synthase
complex, is shown here to have a negative effect
on growth and to produce an alteration on morphology
when added to M. rouxii growth culture
medium. This result has an important impact on
the possible participation of b-1,3-glucans on the
regulation of morphology of zygomycetes.b-1,3-
glucans are major components of the cell wall.
Even though glucans have not been detected in
zygomycetes, caspofungin, an echinochandin
known to be an inhibitor of b-1,3-glucan synthase
complex, is shown here to have a negative effect
on growth and to produce an alteration on morphology
when added to M. rouxii growth culture
medium. This result has an important impact on
the possible participation of b-1,3-glucans on the
regulation of morphology of zygomycetes.b-1,3-glucan synthase
complex, is shown here to have a negative effect
on growth and to produce an alteration on morphology
when added to M. rouxii growth culture
medium. This result has an important impact on
the possible participation of b-1,3-glucans on the
regulation of morphology of zygomycetes.M. rouxii growth culture
medium. This result has an important impact on
the possible participation of b-1,3-glucans on the
regulation of morphology of zygomycetes.b-1,3-glucans on the
regulation of morphology of zygomycetes.