Amino acid transport in Neurospora crassa. II. Properties of a basic amino acid transport system

Pall, Martin L.

doi:10.1016/0005-2736(70)90044-1

Cited by 65 publications

(28 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The observed inhibition pattern indicates that the specificity of this permease is determined mainly by the presence and structural configuration of the ␣-amine group. These observations confirm studies observed in mycelial suspensions and are consistent with the narrow substrate specificity described for system VI, the arginine/lysine permease (9,20). Effect of ionophores on arginine uptake.…”

Section: Resultssupporting

confidence: 90%

“…Both cells and hybrid membranes hardly showed any uptake of leucine and methionine, both typical substrates for the GAP (6). Moreover, the narrow substrate specificity of the system described in this paper (Table 1) agrees with the specificity described for the arginine/lysine permease (system VI) (9,20). In analogy to Saccharomyces cerevisiae, a symport stoichiometry of 1 H ϩ per amino acid was determined for the basic amino acid permease (5,19).…”

Section: Discussionsupporting

confidence: 81%

“…To study plasma membrane-located transport systems in P. chrysogenum, we have developed a model system devoid of metabolic activities by fusing membrane vesicles with liposomes containing the mitochondrial beef heart cytochrome c oxidase (4, 7). We have used this hybrid system to analyze the characteristics of the constitutive basic amino acid transport system in vitro (9,20). Several properties of this transport system which were difficult to assess in mycelial suspension could be characterized well in this hybrid system.…”

mentioning

confidence: 99%

“…In N. crassa, five distinct transport systems have been identified, with specificity for aromatic and aliphatic amino acids (system I); aromatic, aliphatic, and basic amino acids (system II); basic amino acids (system III); acidic amino acids (system IV); and L-methionine (system V) (5,8,20,25). Studies with mycelium of P. chrysogenum indicate that this fungus possesses at least six distinct amino acid transport systems (1, 5, 8-10, 11, 24).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Basic amino acid transport in plasma membrane vesicles of Penicillium chrysogenum

et al. 1996

View full text Add to dashboard Cite

The characteristics of the basic amino acid permease (system VI) of the filamentous fungus Penicillium chrysogenum were studied in plasma membranes fused with liposomes containing the beef heart mitochondrial cytochrome c oxidase. In the presence of reduced cytochrome c, the hybrid membranes accumulated the basic amino acids arginine and lysine. Inhibition studies with analogs revealed a narrow substrate specificity. Within the external pH range of 5.5 to 7.5, the transmembrane electrical potential (⌬) functions as the main driving force for uphill transport of arginine, although a low level of uptake was observed when only a transmembrane pH gradient was present. It is concluded that the basic amino acid permease is a H ؉ symporter. Quantitative analysis of the steady-state levels of arginine uptake in relation to the proton motive force suggests a H ؉ -arginine symport stoichiometry of one to one. Efflux studies demonstrated that the basic amino acid permease functions in a reversible manner.Amino acids are utilized by fungi as primary or secondary nitrogen sources or as building blocks for the synthesis of proteins and peptides. Systems involved in the translocation of amino acids across the plasma membrane have been studied in only a few filamentous fungi (5,8,25). Of these fungi, Neurospora crassa, Aspergillus nidulans, and, to a lesser extent, Penicillium chrysogenum are genetically and biochemically the most extensively characterized species. Two distinct classes of plasma membrane-located amino acid permeases are found in filamentous fungi: systems that catalyze the uptake of structurally related amino acids with a broad substrate specificity, such as the general amino acid permeases of plant and animal cells (2,15,18), and systems with a narrow substrate specificity, such as bacterial amino acid transporters (22).Fungi show a peculiar substrate specificity in their amino acid transport systems, and multiple transport mechanisms seem to exist for several amino acids. In N. crassa, five distinct transport systems have been identified, with specificity for aromatic and aliphatic amino acids (system I); aromatic, aliphatic, and basic amino acids (system II); basic amino acids (system III); acidic amino acids (system IV); and L-methionine (system V) (5,8,20,25). Studies with mycelium of P. chrysogenum indicate that this fungus possesses at least six distinct amino acid transport systems (1, 5, 8-10, 11, 24). Most of these systems are specific for one amino acid and analogs, except for system III, which is a general amino acid permease, and system IV, which transports acidic amino acids only (8, 10). Amino acid transporters of fungi are assumed to possess some typical properties: (i) they seem to function unidirectionally; i.e., only uphill transport is observed, while efflux or countertransport of the accumulated amino acids is not detected (8, 19); and (ii) their activity is regulated by transinhibition, i.e., a high internal concentration of an amino acid appears to lower the activity of the transport syst...

show abstract

Section: Resultssupporting

confidence: 90%

Section: Discussionsupporting

confidence: 81%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Basic amino acid transport in plasma membrane vesicles of Penicillium chrysogenum

et al. 1996

View full text Add to dashboard Cite

show abstract

“…The auxotrophic strain prol-3 of Neurospora crassa grows on proline (Vogel & Bonner, 1954)~ as well as on arginine and ornithine, through the action of a general amino acid permease (Pall, 1969(Pall, , 1970Shchez, Martinez & Mora, 1972), an arginase (Castaiieda, Martuscelli & Mora, 1967;Davis, Lawless & Port, 1970) and an ornithine-6-transaminase (Davis & Mora, 1968). These enzymes lead to the formation of glutamic acid and glutamic acid y-semialdehyde, a proline precursor which strain prol-3 is unable to synthesize by the normal biosynthetic pathway (Vogel & Bonner, 1954).…”

Section: Introductionmentioning

confidence: 99%

Effect of the Deprivation of Amino Acids on Conidia of Neurospora crassa

Espı́n¹,

Mora²

1978

Journal of General Microbiology

View full text Add to dashboard Cite

Characterization of Vacuolar Arginine Uptake and Amino Acid Efflux inNeurospora crassaUsing Cupric Ion to Permeabilize the Plasma Membrane

Keenan

Weiss

1997

Fungal Genetics and Biology

View full text Add to dashboard Cite

Amino acid transport in Neurospora crassa. II. Properties of a basic amino acid transport system

Cited by 65 publications

References 15 publications

Basic amino acid transport in plasma membrane vesicles of Penicillium chrysogenum

Basic amino acid transport in plasma membrane vesicles of Penicillium chrysogenum

Effect of the Deprivation of Amino Acids on Conidia of Neurospora crassa

Characterization of Vacuolar Arginine Uptake and Amino Acid Efflux inNeurospora crassaUsing Cupric Ion to Permeabilize the Plasma Membrane

Contact Info

Product

Resources

About