Inhibitory plant serpins with a sequence of three glutamine residues in the reactive center
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Jørn Hejgaard
Abstract
Serpins appear to be ubiquitous in eukaryotes, except fungi, and are also present in some bacteria, archaea and viruses. Inhibitory serpins with a glutamine as the reactive-center P1 residue have been identified exclusively in a few plant species. Unique serpins with a reactive center sequence of three Gln residues at P3-P1 or P2-P1′ were isolated from barley and wheat grain, respectively. Barley BSZ3 was an irreversible inhibitor of chymotrypsin, with a second-order association rate constant for complex formation ka′ of the order of 104 M-1 s-1; however, only a minor fraction of the serpin molecules reacted with chymotrypsin, with the majority insensitive to cleavage in the reactive center loop. Wheat WSZ3 was cleaved specifically at P8 Thr and was not an inhibitor of chymotrypsin. These reactive-center loops may have evolved conformations that are optimal as inhibitory baits for proeinases that specifically degrade storage prolamins containing Gln-rich repetitive sequences, most likely for digestive proteinases of insect pests or fungal pathogens that infect cereals. An assembled full-length amino acid sequence of a serpin expressed in cotton boll fiber (GaZ1) included conserved regions essential for serpin-proteinase interaction, suggesting inhibitory capacity at a putative reactive center P2-P2′ with a sequence of four Gln residues.
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©2005 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Highlight: RNA Biochemistry
- microRNA-guided posttranscriptional gene regulation
- How to find small non-coding RNAs in bacteria
- Species-specific antibiotic-ribosome interactions: implications for drug development
- The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
- Alternative pre-mRNA splicing in the human system: unexpected role of repetitive sequences as regulatory elements
- 6S RNA – an ancient regulator of bacterial RNA polymerase rediscovered
- RNA thermometers are common in α- and γ-proteobacteria
- Inhibition of mRNA deadenylation and degradation by ultraviolet light
- Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins
- Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II
- Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
- Inhibitory plant serpins with a sequence of three glutamine residues in the reactive center
- Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
- Acknowledgement
- Contents Biological Chemistry Volume 386, 2005
- Author Index
- Subject Index
Articles in the same Issue
- Highlight: RNA Biochemistry
- microRNA-guided posttranscriptional gene regulation
- How to find small non-coding RNAs in bacteria
- Species-specific antibiotic-ribosome interactions: implications for drug development
- The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
- Alternative pre-mRNA splicing in the human system: unexpected role of repetitive sequences as regulatory elements
- 6S RNA – an ancient regulator of bacterial RNA polymerase rediscovered
- RNA thermometers are common in α- and γ-proteobacteria
- Inhibition of mRNA deadenylation and degradation by ultraviolet light
- Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins
- Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II
- Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
- Inhibitory plant serpins with a sequence of three glutamine residues in the reactive center
- Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
- Acknowledgement
- Contents Biological Chemistry Volume 386, 2005
- Author Index
- Subject Index