Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly
The biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Rec...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Fundação Oswaldo Cruz (FIOCRUZ)
2018-07-01
|
| Series: | Memorias do Instituto Oswaldo Cruz |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762018000900401&lng=en&tlng=en |
| _version_ | 1797702977941667840 |
|---|---|
| author | Luis Ernesto Contreras-Rodríguez Catherin Yizet Marin-Mogollon Lina Marcela Sánchez-Mejía María Helena Ramírez-Hernández |
| author_facet | Luis Ernesto Contreras-Rodríguez Catherin Yizet Marin-Mogollon Lina Marcela Sánchez-Mejía María Helena Ramírez-Hernández |
| author_sort | Luis Ernesto Contreras-Rodríguez |
| collection | DOAJ |
| description | The biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Recently, the NMNAT of Plasmodium falciparum (PfNMNAT) has been identified as a pharmacological target. The enzymatic characterisation, cellular location, and tertiary structure of the PfNMNAT protein have been reported. Nonetheless, its quaternary structure remains to be explored. The present study describes the oligomeric assembly of the 6 x His-PfNMNAT recombinant protein using immobilised metal affinity chromatography coupled with size exclusion chromatography (SEC) and native protein electrophoresis combined with Ferguson plot graphing. These chromatographic approaches resulted in the elution of an active monomer from the SEC column, whereas the Ferguson plot indicated a dimeric assembly of the 6 x His-PfNMNAT protein. |
| first_indexed | 2024-03-12T04:57:47Z |
| format | Article |
| id | doaj.art-85f103a7558545e6aa2fdf5960dbaa69 |
| institution | Directory Open Access Journal |
| issn | 1678-8060 |
| language | English |
| last_indexed | 2024-03-12T04:57:47Z |
| publishDate | 2018-07-01 |
| publisher | Fundação Oswaldo Cruz (FIOCRUZ) |
| record_format | Article |
| series | Memorias do Instituto Oswaldo Cruz |
| spelling | doaj.art-85f103a7558545e6aa2fdf5960dbaa692023-09-03T09:14:40ZengFundação Oswaldo Cruz (FIOCRUZ)Memorias do Instituto Oswaldo Cruz1678-80602018-07-01113910.1590/0074-02760180073S0074-02762018000900401Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assemblyLuis Ernesto Contreras-RodríguezCatherin Yizet Marin-MogollonLina Marcela Sánchez-MejíaMaría Helena Ramírez-HernándezThe biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Recently, the NMNAT of Plasmodium falciparum (PfNMNAT) has been identified as a pharmacological target. The enzymatic characterisation, cellular location, and tertiary structure of the PfNMNAT protein have been reported. Nonetheless, its quaternary structure remains to be explored. The present study describes the oligomeric assembly of the 6 x His-PfNMNAT recombinant protein using immobilised metal affinity chromatography coupled with size exclusion chromatography (SEC) and native protein electrophoresis combined with Ferguson plot graphing. These chromatographic approaches resulted in the elution of an active monomer from the SEC column, whereas the Ferguson plot indicated a dimeric assembly of the 6 x His-PfNMNAT protein.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762018000900401&lng=en&tlng=enNMNAToligomersPlasmodium falciparum |
| spellingShingle | Luis Ernesto Contreras-Rodríguez Catherin Yizet Marin-Mogollon Lina Marcela Sánchez-Mejía María Helena Ramírez-Hernández Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly Memorias do Instituto Oswaldo Cruz NMNAT oligomers Plasmodium falciparum |
| title | Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly |
| title_full | Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly |
| title_fullStr | Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly |
| title_full_unstemmed | Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly |
| title_short | Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly |
| title_sort | structural insights into plasmodium falciparum nicotinamide mononucleotide adenylyltransferase oligomeric assembly |
| topic | NMNAT oligomers Plasmodium falciparum |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762018000900401&lng=en&tlng=en |
| work_keys_str_mv | AT luisernestocontrerasrodriguez structuralinsightsintoplasmodiumfalciparumnicotinamidemononucleotideadenylyltransferaseoligomericassembly AT catherinyizetmarinmogollon structuralinsightsintoplasmodiumfalciparumnicotinamidemononucleotideadenylyltransferaseoligomericassembly AT linamarcelasanchezmejia structuralinsightsintoplasmodiumfalciparumnicotinamidemononucleotideadenylyltransferaseoligomericassembly AT mariahelenaramirezhernandez structuralinsightsintoplasmodiumfalciparumnicotinamidemononucleotideadenylyltransferaseoligomericassembly |