| Full text | |
| Author(s): |
Sculaccio, Susana Andrea
[1]
;
Napolitano, Hamilton Barbosa
[1, 2]
;
Beltramini, Leila Maria
[1]
;
Oliva, Glaucius
[1]
;
Carrilho, Emanuel
[3]
;
Thiemann, Otavio Henrique
[1]
Total Authors: 6
|
| Affiliation: | [1] Univ Sao Paulo, Inst Fis Sao Carlos, Dept Genet & Evolucao, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Estadual Goias, BR-75001970 Anapolis, Go - Brazil
[3] Univ Sao Paulo, Inst Quim Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | PLANT MOLECULAR BIOLOGY REPORTER; v. 26, n. 4, p. 301-315, DEC 2008. |
| Web of Science Citations: | 4 |
| Abstract | |
Phosphoribosyl pyrophosphate synthetase (PRS-EC:2.7.6.1) is an important enzyme present in several metabolic pathways, thus forming a complex family of isoenzymes. However, plant PRS enzymes have not been extensively investigated. In this study, a sugarcane prs gene has been characterized from the Sugar Cane Expressed Sequence Tag Genome Project. This gene contains a 984-bp open reading frame encoding a 328-amino acid protein. The predicted amino acid sequence has 77% and 78% amino acid sequence identity to Arabidopsis thaliana and Spinacia oleracea PRS4, respectively. The assignment of sugarcane PRS as a phosphate-independent PRS isoenzyme (Class II PRS) is verified following enzyme assay and phylogenetic reconstruction of PRS homologues. To gain further insight into the structural framework of the phosphate independence of sugarcane PRS, a molecular model is described. This model reveals the formation of two conserved domains elucidating the structural features involved in sugarcane PRS phosphate independence. The recombinant PRS retains secondary structure elements and a quaternary arrangement consistent with known PRS homologues, based on circular dichroism measurements. (AU) | |
| FAPESP's process: | 99/02874-9 - The sugarcane EST project |
| Grantee: | Otavio Henrique Thiemann |
| Support Opportunities: | Genome Research Grants |