Genetic alterations of ribonuclease-sensitive glycoprotein subunits of amino acid transport systems in Neurospora crassa conidia

Stuart, William D.; DeBusk, A. G.

doi:10.1016/0003-9861(75)90382-3

Cited by 14 publications

(24 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The occurrence of allelic complementation implies that the mtr locus encodes a protein supported by the isolation of a temperaturedependent mtr allele (2). Thus, the active product is an oligomer, which was previously suggested by the binding-protein results of Stuart and DeBusk (3).…”

supporting

confidence: 54%

“…Stuart and DeBusk (3,4) found that mtr-6r and mtr-pm22 have altered amino acid-binding fIr 271S glycoprotein-affinity profiles, and mtr-6r was shown to have an altered tryptic peptide pattern in dialyzed KCI extracts. Our results indimin fail to cate that these mutants do produce a mutant ormplement protein, but their transport capacity is reduced onoverlapor absent.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Genetic and kinetic analysis of Neurospora crassa mtr mutants

Larimer¹,

DeBusk²

1977

J Bacteriol

View full text Add to dashboard Cite

show abstract

supporting

confidence: 54%

mentioning

confidence: 99%

Genetic and kinetic analysis of Neurospora crassa mtr mutants

Larimer¹,

DeBusk²

1977

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Heterokaryons formed between mutants containing these alleles of mtr demonstrate variable restoration of transport by complementation (Larimer and DeBusk 1977), thus indicating that the gene product is a protein that forms a multimeric complex in vivo. Experimental evidence (Stuart and DeBusk 1975; Stuart andWoodward 1975, 1977; Koo and Stuart 1984) supports the suggestion (Stuart 1977) that the gene product of the rntr locus is one participant in a ribonucleoprotein complex that forms the amino acid permease system.…”

Section: Introductionmentioning

confidence: 87%

Cloning of mtr, an amino acid transport gene of Neurospora crassa

K²,

Vollmer³

1988

Genome

View full text Add to dashboard Cite

Translocation of neutral aliphatic and aromatic amino acids across the plasma membrane of the ascomycete Neurospora crassa requires a functional gene product of the mtr locus. Mutations at this locus are defective in transport of those amino acids. We have cloned the mtr+ gene of Neurospora crassa from an ordered cosmid library of genomic DNA and produced a preliminary restriction map of 2.9 kilobases of genomic DNA that encompasses the mtr coding region. We have confirmed that the cloned DNA regions contain the mtr gene sequence by restriction fragment length polymorphism mapping and have determined that the cloned sequence codes for a messenger RNA transcript of approximately 1200 nucleotides in length.

show abstract

mentioning

confidence: 99%

“…It has been reported previously that conidia extracted with KCl show reduced L-arginine transport (19). These KCI extracts contain amino acid-binding glycoproteins that can be purified by affinity chromatography (19). Disappearance of certain fractions is coordinate with the introduction of genetic lesions that reduce amino acid transport (19).…”

mentioning

confidence: 99%

Effects of ribonuclease A on amino acid transport in Neurospora crassa

Stuart¹,

Woodward²

1975

J Bacteriol

View full text Add to dashboard Cite

Incubation of Neurospora crassa conidia with ribonuclease (RNase) A reduces transport of L-phenylalanine by those cells. Under similar conditions, oxidized RNase A, RNase T,, and RNase T2 do not have this effect. Incubation of conidia with active RNase covalently attached to polyacrylamide beads reduces L-phenylalanine transport. This indicates that the site of enzymatic action is at the cell surface. At the lower concentration of enzyme used in this study, incubation with RNase A reduces transport of L-phenylalanine by the general (G) amino acid permease. Increasing the enzyme concentration results in reduction of transport by the neutral aromatic (N)-specific permease. The increased transport activity that accompanies onset of conidial germination is also sensitive to incubation with RNase A. Application of the enzyme to actively transporting cells does not release amino acid transported prior to enzyme addition. Cells cultured on media supplemented with [2-"C]uridine release isotopic activity after RNase A incubation. Analogous treatments with Pronase, RNase T,, RNase T2, or deoxyribonuclease I do not release isotope activity.Pronase treatment does reduce L-phenylalanine transport. Incubation of conidia with RNase A also inhibits germination of those conidia. tion was 0.514 M; and (ii) Vogel salts (23) diluted 100-fold at pH 6.0.Conidia were collected on glass-fiber filters (Whatman GF/C, 2.4 cm) and digested with tissue solubilizer (NCS, Amersham/Searle), and the radioactivity was determined in a Beckman LS-100 scintillation counter with toluene-Omnifluor (New England Nu-41 on August 1, 2020 by guest

show abstract

Genetic alterations of ribonuclease-sensitive glycoprotein subunits of amino acid transport systems in Neurospora crassa conidia

Cited by 14 publications

References 27 publications

Genetic and kinetic analysis of Neurospora crassa mtr mutants

Genetic and kinetic analysis of Neurospora crassa mtr mutants

Cloning of mtr, an amino acid transport gene of Neurospora crassa

Effects of ribonuclease A on amino acid transport in Neurospora crassa

Contact Info

Product

Resources

About