Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii

Moreno, Sílvia; Passeron, Susana

doi:10.1016/0003-9861(80)90287-8

Cited by 39 publications

(18 citation statements)

References 32 publications

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“…However, only one band was detected while running the same sample on a native gel (data not shown). Different intensity of the two bands could be explained by extreme instability of one subunit, as observed also in some other species [14]. Recorded molecular masses are in accordance with the observations of these enzymes from other organisms where the molecular masses of both subunits appear to be close to 50000 [15].…”

Section: Resultssupporting

confidence: 88%

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Evidence for the activation of 6-phosphofructo-1-kinase by cAMP-dependent protein kinase in Aspergillus niger

Legiša

1994

FEMS Microbiology Letters

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The change from pentose phosphate pathway to glycolysis plays a significant role in the physiology of Aspergillus niger during the induction of citric acid accumulation. Evidence is shown for the importance of 6-phosphofructo-1-kinase in this process since it is activated by phosphorylation. By incubating a purified active form of the enzyme together with commercially available alkaline phosphatase, 6-phosphofructo-1-kinase activity was lost after a certain time suggesting that the enzyme was dephosphorylated. Inactive 6-phosphofructo-1-kinase could be isolated from the cells in the early stage of growth in a high citric acid yielding medium. The enzyme was "in vitro" activated by isolated protein kinase in the presence of cAMP, ATP and Mg2+ ions. Additional evidence for covalent phosphorylation of inactive 6-phosphofructo-1-kinase was obtained by incubating both enzymes together with labelled [gamma-32P]ATP. The activating enzyme was partially purified from A. niger mycelium.

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Section: Resultssupporting

confidence: 88%

“…However, its activity could be maintained for a longer period in the presence of 0.2 M NaC1. This compound was found to have multiple effects on cAMP-dependent protein kinase in Mucor rouxii, but above all it is believed that higher ionic strength prevents inactivation of the catalytic subunit [14].…”

Section: Resultsmentioning

confidence: 99%

Evidence for the activation of 6-phosphofructo-1-kinase by cAMP-dependent protein kinase in Aspergillus niger

Legiša

1994

FEMS Microbiology Letters

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“…M. rouxii PKA has been thoroughly characterized (Moreno & Passeron, 1980 ;Moreno et al, 1983 ;Paveto et al, 1989 ;Guthmann et al, 1990) and the levels of its subunits have been measured during the time course of spore germination in rich medium (Rossi & Moreno, 1994).…”

Section: Introductionmentioning

confidence: 99%

Threshold level of protein kinase A activity and polarized growth in Mucor rouxii

2000

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A model system to study the involvement of cAMP-mediated regulation of a cellular process such as hyphal morphogenesis was investigated. Impairment of polarized growth was observed when Mucor rouxii sporangiospores were grown in the presence of N 6 -cAMP analogues and of SQ 65,442, a cAMP phosphodiesterase inhibitor. Together with an effect on isodiametric growth, there was increased pigmentation, increased cell fragility and loss of cell adhesiveness. The total effect on morphology was attained even after adding the compounds shortly before germ-tube emergence ; when added after this time growth continued in a non-polarized form and rounding of the germ tip was observed. The morphological effect was observed under all the nutritional and environmental conditions studied (aerobic conditions and defined medium with maltose or glucose, Casamino acids medium with glucose, or rich medium ; anaerobic conditions with rich medium ; and following a shift from anaerobiosis to aerobiosis). The time of germ-tube emergence, and the size of the cell at this time, was dependent on the growth medium. Protein kinase A (PKA) specific activity was followed during the germination process under three growth conditions. It was found that the total activity of PKA correlated with differentiation and not with growth, and that the total specific activity at the time of germination was the same, independent of the culture medium. The time of germ-tube emergence correlated with the time of attainment of a threshold level of PKA total specific activity. The concentration of dibutyrylcAMP needed to promote isodiametric growth correlated with the total units of activity of PKA to be activated per cell. It was concluded that PKA is involved in the morphogenetic process of the fungus grown under all the nutritional and ambient conditions tested.

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“…The holoenzyme was prepared from mycelial powder; extraction and enzyme purification through DEAE-Sepharose and sucrose gradient centrifugation were performed as described (18). The catalytic subunit was isolated by incubating the holoenzyme with 10 M cAMP and 0.5 M NaCl and by further separation of the C from the R subunit through sedimentation in 5-20% sucrose gradients equilibrated with 0.5 M NaCl and 0.4 M cAMP as described (19).…”

Section: Methodsmentioning

confidence: 99%

Mechanism of Activation of cAMP-Dependent Protein Kinase: In Mucor rouxii the Apparent Specific Activity of the cAMP-Activated Holoenzyme Is Different than That of Its Free Catalytic Subunit

Zaremberg

Donella‐Deana

Moreno

2000

Archives of Biochemistry and Biophysics

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Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii

Cited by 39 publications

References 32 publications

Evidence for the activation of 6-phosphofructo-1-kinase by cAMP-dependent protein kinase in Aspergillus niger

Evidence for the activation of 6-phosphofructo-1-kinase by cAMP-dependent protein kinase in Aspergillus niger

Threshold level of protein kinase A activity and polarized growth in Mucor rouxii

Mechanism of Activation of cAMP-Dependent Protein Kinase: In Mucor rouxii the Apparent Specific Activity of the cAMP-Activated Holoenzyme Is Different than That of Its Free Catalytic Subunit

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