The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants
| Autor: | Tiina Blomster, Jarkko Salojärvi, Julia P. Vainonen, Pinja Jaspers, Jaakko Kangasjärvi, Michael Wrzaczek, Ramesha A. Reddy, Kirk Overmyer |
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| Přispěvatelé: | Biosciences, Plant-Fungal Interactions Group, Receptor-Ligand Signaling Group, Plant ROS-Signalling |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
0106 biological sciences
411 Agriculture and forestry Arabidopsis Protein structure function SALT TOLERANCE 01 natural sciences Conserved sequence Protein structure Gene Expression Regulation Plant Sequence Analysis Protein BINDING 311 Basic medicine TRANSCRIPTION Peptide sequence Conserved Sequence Phylogeny GENE-EXPRESSION Plant Proteins Genetics 0303 health sciences 318 Medical biotechnology GENOME 519 Social and economic geography Multigene Family Poly(ADP-ribose) Polymerases Biotechnology Research Article Protein family lcsh:QH426-470 Sequence analysis lcsh:Biotechnology education Molecular Sequence Data Sequence alignment Biology SEQUENCE 03 medical and health sciences Structure-Activity Relationship lcsh:TP248.13-248.65 Protein Interaction Domains and Motifs WWE DOMAIN Amino Acid Sequence MONO-ADP-RIBOSYLATION Transcription factor 219 Environmental biotechnology 030304 developmental biology Gene Expression Profiling lcsh:Genetics CELL-DEATH ARABIDOPSIS-THALIANA 118 Biological sciences Sequence Alignment 010606 plant biology & botany Transcription Factors |
| Zdroj: | BMC Genomics, Vol 11, Iss 1, p 170 (2010) BMC Genomics |
| ISSN: | 1471-2164 |
| Popis: | Background The SROs (SIMILAR TO RCD-ONE) are a group of plant-specific proteins which have important functions in stress adaptation and development. They contain the catalytic core of the poly(ADP-ribose) polymerase (PARP) domain and a C-terminal RST (RCD-SRO-TAF4) domain. In addition to these domains, several, but not all, SROs contain an N-terminal WWE domain. Results SROs are present in all analyzed land plants and sequence analysis differentiates between two structurally distinct groups; cryptogams and monocots possess only group I SROs whereas eudicots also contain group II. Group I SROs possess an N-terminal WWE domain (PS50918) but the WWE domain is lacking in group II SROs. Group I domain structure is widely represented in organisms as distant as humans (for example, HsPARP11). We propose a unified nomenclature for the SRO family. The SROs are able to interact with transcription factors through the C-terminal RST domain but themselves are generally not regulated at the transcriptional level. The most conserved feature of the SROs is the catalytic core of the poly(ADP-ribose) polymerase (PS51059) domain. However, bioinformatic analysis of the SRO PARP domain fold-structure and biochemical assays of AtRCD1 suggested that SROs do not possess ADP-ribosyl transferase activity. Conclusions The SROs are a highly conserved family of plant specific proteins. Sequence analysis of the RST domain implicates a highly preserved protein structure in that region. This might have implications for functional conservation. We suggest that, despite the presence of the catalytic core of the PARP domain, the SROs do not possess ADP-ribosyl transferase activity. Nevertheless, the function of SROs is critical for plants and might be related to transcription factor regulation and complex formation. |
| Databáze: | OpenAIRE |
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