Histidine uptake in mutant strains of Neurospora crassa via the general transport system for amino acids. Academic Article

abstract

• A transport double mutant of Neurospora crassa has been isolated that has only one of the three transport systems capable of l-histidine uptake. The substrate specificity of the remaining transport system, termed the general transport system, has been fully characterized with regard to the contributions to binding of the side chain, the alpha-amino group, and the carboxylate group. The positively charged alpha-amino group is necessary for binding; the negatively charged carboxylate group is of less importance, since its replacement by a neutral carbonyl functional group does not completely abolish binding. The greatest structural latitude for binding was found in the side chain; affinity for alpha-amino acids was uniformly high except for l-aspartic and l-glutamic acids, l-asparagine, and l-proline. Thus, this transport system is "general" with these restrictions.

authors

• Magill, Clint

published proceedings

• J Bacteriol

author list (cited authors)

• Magill, C. W., Nelson, S. O., D'Ambrosio, S. M., & Glover, G. I.

citation count

• 10

complete list of authors

• Magill, CW||Nelson, SO||D'Ambrosio, SM||Glover, GI

publication date

• March 1973

publisher

• American Society for Microbiology  Publisher

published in

• Journal of Bacteriology  Journal

keywords

• Amino Acids
• Binding Sites
• Biological Transport, Active
• Carbon Isotopes
• Histidine
• Mutation
• Neurospora
• Neurospora Crassa
• Spores, Fungal
• Stereoisomerism

PubMed Central ID

• 4266243

Digital Object Identifier (DOI)

• 10.1128/jb.113.3.1320-1325.1973

start page

• 1320

end page

• 1325

volume

• 113

issue

• 3

URL

• http://dx.doi.org/10.1128/jb.113.3.1320-1325.1973