Characterization of amino acid pools in the vacuolar compartment of Saccharomyces cerevisiae

1974 ◽  
Vol 101 (1) ◽  
pp. 45-57 ◽  
Author(s):  
Andres Wiemken ◽  
Mathias D�rr
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Vacuolar Compartment

scholarly journals Functional Expression and Characterization of Schizosaccharomyces pombe Avt3p as a Vacuolar Amino Acid Exporter in Saccharomyces cerevisiae

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0130542 ◽  
Author(s):  
Soracom Chardwiriyapreecha ◽  
Kunio Manabe ◽  
Tomoko Iwaki ◽  
Miyuki Kawano-Kawada ◽  
Takayuki Sekito ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Schizosaccharomyces Pombe ◽  
Functional Expression

scholarly journals Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene

1999 ◽  
Vol 339 (2) ◽  
pp. 407-411 ◽  
Author(s):  
Vicki OLSEN ◽  
Niamh X. CAWLEY ◽  
Jakob BRANDT ◽  
Michi EGEL-MITANI ◽  
Y. Peng LOH
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Cleavage Sites ◽  
Basic Residue ◽  
Aspartic Proteases ◽  
N Terminus ◽  
High Degree ◽  
Identification And Characterization ◽  
Degree Of Similarity

A new aspartic protease from Saccharomyces cerevisiae, with a high degree of similarity with yapsin 1 and yapsin 2 and a specificity for basic residue cleavage sites of prohormones, has been cloned. This enzyme was named yapsin 3. Expression of a C-terminally truncated non-membrane anchored yapsin 3 in yeast yielded a heterogeneous protein between 135–200 kDa which, upon treatment with endoglycosidase H, migrated as a 60 kDa form. Amino-acid analysis of the N-terminus of expressed yapsin 3 revealed two different N-terminal residues, serine-48 and phenylalanine-54, which followed a dibasic and a monobasic residue respectively. Cleavage of several prohormones by non-anchored yapsin 3 revealed a specificity distinct from that of yapsin 1.

scholarly journals Pex19p, a Farnesylated Protein Essential for Peroxisome Biogenesis

1998 ◽  
Vol 18 (1) ◽  
pp. 616-628 ◽  
Author(s):  
Klaudia Götte ◽  
Wolfgang Girzalsky ◽  
Michael Linkert ◽  
Evelyn Baumgart ◽  
Stefan Kammerer ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Oleic Acid ◽  
Amino Acid ◽  
Matrix Proteins ◽  
Proper Function ◽  
Peroxisome Biogenesis ◽  
Human Ortholog ◽  
Farnesylated Protein

ABSTRACT We report the identification and molecular characterization of Pex19p, an oleic acid-inducible, farnesylated protein of 39.7 kDa that is essential for peroxisome biogenesis in Saccharomyces cerevisiae. Cells lacking Pex19p are characterized by the absence of morphologically detectable peroxisomes and mislocalization of peroxisomal matrix proteins to the cytosol. The human HK33 gene product was identified as the putative human ortholog of Pex19p. Evidence is provided that farnesylation of Pex19p takes place at the cysteine of the C-terminal CKQQ amino acid sequence. Farnesylation of Pex19p was shown to be essential for the proper function of the protein in peroxisome biogenesis. Pex19p was shown to interact with Pex3p in vivo, and this interaction required farnesylation of Pex19p.

scholarly journals Characterization of vacuolar amino acid transporter from Fusarium oxysporum in Saccharomyces cerevisiae

2015 ◽  
Vol 79 (12) ◽  
pp. 1972-1979 ◽  
Author(s):  
Siriporn Lunprom ◽  
Pongsanat Pongcharoen ◽  
Takayuki Sekito ◽  
Miyuki Kawano-Kawada ◽  
Yoshimi Kakinuma ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Fusarium Oxysporum ◽  
Amino Acid Transporter ◽  
Acid Transporter

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

Taxonomic characterization and identification of Saccharomyces cerevisiae D8 for brandy production from pineapple

2018 ◽  
Vol 39 (4) ◽  
pp. 474-482
Author(s):  
Hoang Thi Le Thuong ◽  
Nguyen Quang Hao ◽  
Tran Thi Thuy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Low Ph ◽  
Yeast Strains ◽  
Biological Studies ◽  
Taxonomic Characterization

Eight yeast strains (denoted as D1 to D8) were isolated from samples of natural fermented pineapple. Strain D8 showed highest alcoholic production at low pH and special aroma of pineapple has been chosen for further study. Taxonomic characterization of strain D8 using morphological, biochemical and molecular biological studies confirmed that strain D8  belong to Saccharomycetaceae family, Saccharomycetales order and Saccharomyces cerevisiae species. Therefore, we named this strain as Saccharomyces cerevisiae D8 for further study on Brandy production from pineapple. Citation: Hoang Thi Le Thuong, Nguyen Quang Hao, Tran Thi Thuy, 2017. Taxonomic characterization and identification of Saccharomyces cerevisiae D8 for brandy production from pineapple. Tap chi Sinh hoc, 39(4): 474- 482. DOI: 10.15625/0866-7160/v39n4.10864.*Corresponding author: [email protected] Received 5 December 2016, accepted 12 August 2017

Sign in / Sign up

Export Citation Format

Share Document