D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine

D-ornithine has previously been suggested to enhance the expression of pyrrolysine-containing proteins. We unexpectedly discovered that uptake of D-ornithine results in the insertion of a new amino acid, pyrroline-carboxy-lysine (Pcl) instead of the anticipated pyrrolysine (Pyl). Our feeding and bio...

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Published inNature chemical biology Vol. 7; no. 8; pp. 528 - 530
Main Authors Cellitti, Susan E, Ou, Weijia, Chiu, Hsien-Po, Grünewald, Jan, Jones, David H, Hao, Xueshi, Fan, Qian, Quinn, Lisa L, Ng, Kenneth, Anfora, Andrew T, Lesley, Scott A, Uno, Tetsuo, Brock, Ansgar, Geierstanger, Bernhard H
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 27.04.2011
Subjects
Amino Acid Sequence
Biosynthesis
Chemistry
Escherichia coli
Gene Expression Regulation - physiology
HEK293 Cells
Humans
Lysine - analogs & derivatives
Lysine - biosynthesis
Lysine - chemistry
Methanosarcina - genetics
Methanosarcina - metabolism
Molecular Structure
Ornithine - chemistry
Ornithine - metabolism
Ornithine - pharmacology
Plasmids
Promoter Regions, Genetic
Proteins
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Summary:D-ornithine has previously been suggested to enhance the expression of pyrrolysine-containing proteins. We unexpectedly discovered that uptake of D-ornithine results in the insertion of a new amino acid, pyrroline-carboxy-lysine (Pcl) instead of the anticipated pyrrolysine (Pyl). Our feeding and biochemical studies point to specific roles of the poorly understood Pyl biosynthetic enzymes PylC and PylD in converting L-lysine and D-ornithine to Pcl and confirm intermediates in the biosynthesis of Pyl.
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ISSN:1552-4450
1552-4469
DOI:10.1038/nchembio.586