Biology subjects

Koncitikova, R.

Publications and source records attributed to Koncitikova, R..

2 recordsLinked to original sources

bioRxiv2026

Insight into GABA shunt-associated aldehyde dehydrogenases (ALDH) and stress responses of ALDH superfamily in moss and barley

We explored the expression of the aldehyde dehydrogenase (ALDH) superfamily in two model plants, Physcomitrium patens (moss) and Hordeum vulgare (barley), under various stress conditions. The ALDH enzymes are crucial for oxidizing aldehydes to carboxylic acids and are involved in multiple metabolic pathways. We found significant differences in enzyme expression between moss and barley within the same ALDH families. We then focused on the ALDH5, ALDH10, and ALDH21 families, which are part of the {gamma}-aminobutyric acid (GABA) shunt, noting that the ALDH21 family is absent in barley. The kinetic properties of ALDH10 and ALDH5 enzymes were analyzed, revealing that PpALDH5F1 exhibits high specificity for succinic semialdehyde (SSAL), a product of GABA. The crystal structure of PpALDH5F1 identified key residues for SSAL binding. Knockout mutants of moss aldh5F2, aldh10A1, and aldh21A1 showed slightly smaller colonies than the wild-type. GABA and glutamate levels were elevated in aldh5F2 and aldh21A1 knockouts due to a partially blocked GABA shunt pathway, while aldh10A1 knockout showed no changes in GABA levels. Transcriptomic data revealed a link between several genes, including six upregulated glutathione-S-transferase genes in all three aldh knockouts, suggesting a direct compensatory mechanism for oxidative stress protection via conjugation of undegraded aldehydes to glutathione. HighlightMoss knockouts of GABA shunt-associated aldehyde dehydrogenases display slower growth, changes in levels of glutamate, glutamine and GABA, and result in upregulation of several unique glutathione-S-transferase genes.

plant biology↗

bioRxiv2024

The monomer/dimer switch modulates the activity of plant adenosine kinase

HighlightThe switch from active monomers to inactive dimers in plant ADKs impacts overall enzyme activity and represents a novel negative feedback-loop mechanism to maintain steady levels of adenosine and AMP. Adenosine undergoes ATP-dependent phosphorylation catalyzed by adenosine kinase (ADK). In plants, ADK also phosphorylates cytokinin ribosides, transport forms of the hormone. Here, we investigated the substrate preferences, oligomeric states and structures of ADKs from moss (Physcomitrella patens) and maize (Zea mays) alongside metabolomic and phenotypic analyses. We showed that dexamethasone-inducible ZmADK overexpressor lines in Arabidopsis can benefit from a higher number of lateral roots and larger root areas under nitrogen starvation. We discovered that maize and moss enzymes can form dimers upon increasing protein concentration, setting them apart from the monomeric human and protozoal ADKs. Structural and kinetic analyses revealed a catalytically inactive unique dimer. Within the dimer, both active sites are mutually blocked. The activity of moss ADKs, exhibiting a higher propensity to dimerize, was tenfold lower compared to maize ADKs. Two monomeric structures in a ternary complex highlight the characteristic transition from an open to a closed state upon substrate binding. This suggests that the oligomeric state switch can modulate the activity of moss ADKs and likely other plant ADKs. Moreover, dimer association represents a novel negative feedback mechanism, helping to maintain steady levels of adenosine and AMP.

plant biology↗