An analysis of the sequence of part of the right arm of chromosome II of S. cerevisiae reveals new genes encoding an amino-acid permease and a carboxypeptidase

1994 ◽  
Vol 26 (1) ◽  
pp. 1-7 ◽  
Author(s):  
F. Nasr ◽  
A. -M. B�cam ◽  
E. Grzybowska ◽  
M. Zagulski ◽  
P. P. Slonimski ◽  
...  
2004 ◽  
Vol 70 (9) ◽  
pp. 5315-5322 ◽  
Author(s):  
M. Andrea Azcarate-Peril ◽  
Eric Altermann ◽  
Rebecca L. Hoover-Fitzula ◽  
Raul J. Cano ◽  
Todd R. Klaenhammer

ABSTRACT Amino acid decarboxylation-antiporter reactions are one of the most important systems for maintaining intracellular pH between physiological limits under acid stress. We analyzed the Lactobacillus acidophilus NCFM complete genome sequence and selected four open reading frames with similarities to genes involved with decarboxylation reactions involved in acid tolerance in several microorganisms. Putative genes encoding an ornithine decarboxylase, an amino acid permease, a glutamate γ-aminobutyrate antiporter, and a transcriptional regulator were disrupted by insertional inactivation. The ability of L. acidophilus to survive low-pH conditions, such as those encountered in the stomach or fermented dairy foods, was investigated and compared to the abilities of early- and late-stationary-phase cells of the mutants by challenging them with a variety of acidic conditions. All of the integrants were more sensitive to low pH than the parental strain. Interestingly, each integrant also exhibited an adaptive acid response during logarithmic growth, indicating that multiple mechanisms are present and orchestrated in L. acidophilus in response to acid challenge.


1994 ◽  
Vol 14 (10) ◽  
pp. 6597-6606 ◽  
Author(s):  
A Schmidt ◽  
M N Hall ◽  
A Koller

The macrocyclic lactone FK506 exerts immunosuppressive effects on T lymphocytes by interfering with signal transduction leading to T-cell activation and also inhibits the growth of eukaryotic microorganisms, including Saccharomyces cerevisiae. We reported previously that an FK506-sensitive target in S. cerevisiae is required for amino acid import and that overexpression of two new genes, TAT1 and TAT2 (formerly called TAP1 and TAP2), confers resistance to the drug. Here we report that TAT1 and TAT2 encode novel members of the yeast amino acid permease family composed of integral membrane proteins that share 30 to 40% identity. TAT1 is the tyrosine high-affinity transporter, which also mediates low-affinity or low-capacity uptake of tryptophan. TAT2 is the tryptophan high-affinity transporter. FK506 does not reduce the levels of TAT1 and TAT2 transcripts, indicating that the inhibition of amino acid transport by the drug is posttranscriptional.


2001 ◽  
Vol 183 (18) ◽  
pp. 5325-5333 ◽  
Author(s):  
Peter J. M. Steenbakkers ◽  
Xin-Liang Li ◽  
Eduardo A. Ximenes ◽  
Jorik G. Arts ◽  
Huizhong Chen ◽  
...  

ABSTRACT A method is presented for the specific isolation of genes encoding cellulosome components from anaerobic fungi. The catalytic components of the cellulosome of anaerobic fungi typically contain, besides the catalytic domain, mostly two copies of a 40-amino-acid cysteine-rich, noncatalytic docking domain (NCDD) interspaced by short linkers. Degenerate primers were designed to anneal to the highly conserved region within the NCDDs of the monocentric fungusPiromyces sp. strain E2 and the polycentric fungusOrpinomyces sp. strain PC-2. Through PCR using cDNA fromOrpinomyces sp. and genomic DNA fromPiromyces sp. as templates, respectively, 9 and 19 PCR products were isolated encoding novel NCDD linker sequences. Screening of an Orpinomyces sp. cDNA library with four of these PCR products resulted in the isolation of new genes encoding cellulosome components. An alignment of the partial NCDD sequence information obtained and an alignment of database-accessible NCDD sequences, focusing on the number and position of cysteine residues, indicated the presence of three structural subfamilies within fungal NCDDs. Furthermore, evidence is presented that the NCDDs in CelC from the polycentric fungus Orpinomyces sp. strain PC-2 specifically recognize four proteins in a cellulosome preparation, indicating the presence of multiple scaffoldins.


Yeast ◽  
1993 ◽  
Vol 9 (7) ◽  
pp. 797-806 ◽  
Author(s):  
Françoise Bussereau ◽  
Laurent Mallet ◽  
Michel Jacquet ◽  
Laurent Gaillon
Keyword(s):  

2001 ◽  
Vol 183 (18) ◽  
pp. 5414-5425 ◽  
Author(s):  
Jamie M. Bacher ◽  
Andrew D. Ellington

ABSTRACT Escherichia coli isolates that were tolerant of incorporation of high proportions of 4-fluorotryptophan were evolved by serial growth. The resultant strain still preferred tryptophan for growth but showed improved growth relative to the parental strain on other tryptophan analogues. Evolved clones fully substituted fluorotryptophan for tryptophan in their proteomes within the limits of mass spectral and amino acid analyses. Of the genes sequenced, many genes were found to be unaltered in the evolved strain; however, three genes encoding enzymes involved in tryptophan uptake and utilization were altered: the aromatic amino acid permease (aroP) and tryptophanyl-tRNA synthetase (trpS) contained several amino acid substitutions, and the tyrosine repressor (tyrR) had a nonsense mutation. While kinetic analysis of the tryptophanyl-tRNA synthetase suggests discrimination against 4-fluorotryptophan, an analysis of the incorporation and growth patterns of the evolved bacteria suggest that other mutations also aid in the adaptation to the tryptophan analogue. These results suggest that the incorporation of unnatural amino acids into organismal proteomes may be possible but that extensive evolution may be required to reoptimize proteins and metabolism to accommodate such analogues.


Yeast ◽  
1994 ◽  
Vol 10 (9) ◽  
pp. 1227-1234 ◽  
Author(s):  
M. Zagulski ◽  
A-M Bécam ◽  
E. Grzybowska ◽  
F. Lacroute ◽  
A. Migdalski ◽  
...  

1994 ◽  
Vol 14 (10) ◽  
pp. 6597-6606
Author(s):  
A Schmidt ◽  
M N Hall ◽  
A Koller

The macrocyclic lactone FK506 exerts immunosuppressive effects on T lymphocytes by interfering with signal transduction leading to T-cell activation and also inhibits the growth of eukaryotic microorganisms, including Saccharomyces cerevisiae. We reported previously that an FK506-sensitive target in S. cerevisiae is required for amino acid import and that overexpression of two new genes, TAT1 and TAT2 (formerly called TAP1 and TAP2), confers resistance to the drug. Here we report that TAT1 and TAT2 encode novel members of the yeast amino acid permease family composed of integral membrane proteins that share 30 to 40% identity. TAT1 is the tyrosine high-affinity transporter, which also mediates low-affinity or low-capacity uptake of tryptophan. TAT2 is the tryptophan high-affinity transporter. FK506 does not reduce the levels of TAT1 and TAT2 transcripts, indicating that the inhibition of amino acid transport by the drug is posttranscriptional.


Yeast ◽  
1994 ◽  
Vol 10 (S1994A) ◽  
pp. S1-S11 ◽  
Author(s):  
A.-M. Bécam ◽  
C. Cullin ◽  
E. Grzybowska ◽  
F. Lacroute ◽  
F. Nasr ◽  
...  

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