The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plantsReport as inadecuate




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BMC Genomics

, 11:170

First Online: 12 March 2010Received: 06 November 2009Accepted: 12 March 2010

Abstract

BackgroundThe 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 polyADP-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.

ResultsSROs 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 polyADP-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.

ConclusionsThe 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.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2164-11-170 contains supplementary material, which is available to authorized users.

Pinja Jaspers, Kirk Overmyer, Michael Wrzaczek contributed equally to this work.

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Author: Pinja Jaspers - Kirk Overmyer - Michael Wrzaczek - Julia P Vainonen - Tiina Blomster - Jarkko Salojärvi - Ramesha A Redd

Source: https://link.springer.com/article/10.1186/1471-2164-11-170



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