Somatic hybridization of amino acid analogue-resistant cell lines of potato (Solanum tuberosum L.) by electrofusion

1987 ◽  
Vol 73 (3) ◽  
pp. 451-458 ◽  
Author(s):  
S. E. de Vries ◽  
E. Jacobsen ◽  
M. G. K. Jones ◽  
A. E. H. M. Loonen ◽  
M. J. Tempelaar ◽  
...  
Keyword(s):  
Solanum Tuberosum ◽  
Amino Acid ◽  
Cell Lines ◽  
Somatic Hybridization ◽  
Solanum Tuberosum L ◽  
Resistant Cell ◽  
Amino Acid Analogue ◽  
Acid Analogue

scholarly journals Chitin-binding proteins in potato (Solanum tuberosum L.) tuber. Characterization, immunolocalization and effects of wounding

1992 ◽  
Vol 283 (3) ◽  
pp. 813-821 ◽  
Author(s):  
D J Millar ◽  
A K Allen ◽  
C G Smith ◽  
C Sidebottom ◽  
A R Slabas ◽  
...  
Keyword(s):  
Solanum Tuberosum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Proteins ◽  
Solanum Tuberosum L ◽  
Major Protein ◽  
Post Translational Modification ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Tubers of potato (Solanum tuberosum L.) contain a number of chitin-binding proteins which have possible functions in defence against pathogens. A major protein of the tuber is the chitin-binding lectin which has been further characterized with respect to its antigenicity and N-terminal amino acid sequence. By using an antiserum monospecific for tuber lectin in unwounded potato the protein was found in the cytoplasm and vacuole, unusually for a hydroxyproline-rich glycoprotein, but consistent with its soluble nature in subcellular extracts. Little increased synthesis of the lectin precursor or the post-translationally modified form could be demonstrated in excised potato tuber discs. However, after wounding there is increased synthesis of another hydroxyproline-containing glycoprotein of Mr 57,000, which binds to chitin and shares common epitopes with the lectin. In comparison with the tuber lectin, this novel glycoprotein contains less hydroxyproline, but from its overall composition it is clearly not an underhydroxylated form of the tuber lectin. It differed in its N-terminal amino acid sequence and was much less glycosylated, although arabinose was still present. Synthesis of the Mr-57,000 polypeptide began after the initial burst of protein synthesis and increased, reaching a peak at 24 h after wounding. The protein was produced with its enzymes of post-translational modification, prolyl hydroxylase and arabinosyltransferase, concomitantly with the marker enzymes for wounding, phenylalanine ammonia-lyase and membrane-bound phenol oxidase and peroxidase.

scholarly journals Isolation and characterization of a new class of amino-acid-analogue-resistant mutants inAspergillus nidulansusing reduced carbon flow

1979 ◽  
Vol 34 (2) ◽  
pp. 121-130 ◽  
Author(s):  
Mahavir Singh ◽  
Umakant Sinha
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acids ◽  
Sole Source ◽  
Amino Acid Analogue ◽  
Linkage Groups ◽  
Isolation And Characterization ◽  
Acid Analogue ◽  
Amino Acid Analogues ◽  
Resistant Mutants ◽  
Growth Requirement

SUMMARYFour recessive amino-acid-analogue-resistant mutants were isolated on a medium containing acetate as the sole carbon source and the amino acid analogues p-fluorophenylalanine and ethionine. None of the mutants showed any growth requirement. Analysis of growth on media containing an amino acid as the sole nitrogen source indicated that two mutants out of the four possess normal systems for utilization of acidic, neutral, basic and aromatic amino acids. The mutantsfpa70 andfpa71 showed reduced growth on tryptophan as the sole source of nitrogen. Three new loci, identified after preliminary genetic analysis, were located on three linkage groups: one each on linkage groups I, VI and VIII.

scholarly journals Growth induced translocation effectively directs an amino acid analogue to developing zones in Agaricus bisporus

2020 ◽  
Vol 124 (12) ◽  
pp. 1013-1023 ◽  
Author(s):  
Koen C. Herman ◽  
Han A.B. Wösten ◽  
Mark D. Fricker ◽  
Robert-Jan Bleichrodt
Keyword(s):  
Amino Acid ◽  
Agaricus Bisporus ◽  
Amino Acid Analogue ◽  
Acid Analogue

In vitro selection of salt tolerant cell lines in Solanum tuberosum L.

2007 ◽  
Vol 51 (4) ◽  
pp. 728-734 ◽  
Author(s):  
F. Queiros ◽  
F. Fidalgo ◽  
I. Santos ◽  
R. Salema
Keyword(s):  
Solanum Tuberosum ◽  
Cell Lines ◽  
In Vitro Selection ◽  
Solanum Tuberosum L ◽  
Salt Tolerant ◽  
Tolerant Cell ◽  
Selection Of
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