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Deubiquitylating enzymes and their emerging role in plant biology.

Isono E, Nagel MK - Front Plant Sci (2014)

Bottom Line: One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets.DUBs are also essential for processing ubiquitin precursors and are important for recycling ubiquitin molecules from target proteins prior to their degradation and thereby maintaining the free ubiquitin pool in the cell.Here, we will discuss the five different DUB families (USP/UBP, UCH, JAMM, OTU, and MJD) and their known biochemical and physiological roles in plants.

View Article: PubMed Central - PubMed

Affiliation: Department of Plant Systems Biology, Technische Universität München Freising, Germany.

ABSTRACT
Ubiquitylation is a reversible post-translational modification that is involved in various cellular pathways and that thereby regulates various aspects of plant biology. For a long time, functional studies of ubiquitylation have focused on the function of ubiquitylating enzymes, especially the E3 ligases, rather than deubiquitylating enzymes (DUBs) or ubiquitin isopeptidases, enzymes that hydrolyze ubiquitin chains. One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets. However, recent studies have revealed that DUBs also actively participate in controlling cellular events and thus play pivotal roles in plant development and growth. DUBs are also essential for processing ubiquitin precursors and are important for recycling ubiquitin molecules from target proteins prior to their degradation and thereby maintaining the free ubiquitin pool in the cell. Here, we will discuss the five different DUB families (USP/UBP, UCH, JAMM, OTU, and MJD) and their known biochemical and physiological roles in plants.

No MeSH data available.


Phylogenetic analyses of Arabidopsis UBP-, JAMM-, and OTU-domain proteinases. A Neighbor-Joining consensus tree based on amino acid sequences surrounding the catalytic domain for Arabidopsis UBP- (A), JAMM- (B) and OTU- (C) domain proteins is shown. Scale bars indicate 0.5 aa substitutions per site. DUBs mentioned in the text are highlighted in blue. Note that CSN5A and CSN5B shown in (B) are deneddylating- and not deubiquitylating enzymes.
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Figure 2: Phylogenetic analyses of Arabidopsis UBP-, JAMM-, and OTU-domain proteinases. A Neighbor-Joining consensus tree based on amino acid sequences surrounding the catalytic domain for Arabidopsis UBP- (A), JAMM- (B) and OTU- (C) domain proteins is shown. Scale bars indicate 0.5 aa substitutions per site. DUBs mentioned in the text are highlighted in blue. Note that CSN5A and CSN5B shown in (B) are deneddylating- and not deubiquitylating enzymes.

Mentions: The UBPs form the largest subfamily of cysteine protease DUBs in Arabidopsis with 27 members that can be classified in 14 subfamilies based on their domain organization (Yan et al., 2000; Figure 2A). Most of the UBPs have additionally to their catalytic domain further domains that enable them to interact with different proteins, allowing UBPs to be involved in a broad range of biological processes. However, to date, the molecular functions of UBPs are far from being well resolved in plants, UBP26 being the only member among this family for which the target protein, Histone H2B, is identified (Sridhar et al., 2007).


Deubiquitylating enzymes and their emerging role in plant biology.

Isono E, Nagel MK - Front Plant Sci (2014)

Phylogenetic analyses of Arabidopsis UBP-, JAMM-, and OTU-domain proteinases. A Neighbor-Joining consensus tree based on amino acid sequences surrounding the catalytic domain for Arabidopsis UBP- (A), JAMM- (B) and OTU- (C) domain proteins is shown. Scale bars indicate 0.5 aa substitutions per site. DUBs mentioned in the text are highlighted in blue. Note that CSN5A and CSN5B shown in (B) are deneddylating- and not deubiquitylating enzymes.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3928566&req=5

Figure 2: Phylogenetic analyses of Arabidopsis UBP-, JAMM-, and OTU-domain proteinases. A Neighbor-Joining consensus tree based on amino acid sequences surrounding the catalytic domain for Arabidopsis UBP- (A), JAMM- (B) and OTU- (C) domain proteins is shown. Scale bars indicate 0.5 aa substitutions per site. DUBs mentioned in the text are highlighted in blue. Note that CSN5A and CSN5B shown in (B) are deneddylating- and not deubiquitylating enzymes.
Mentions: The UBPs form the largest subfamily of cysteine protease DUBs in Arabidopsis with 27 members that can be classified in 14 subfamilies based on their domain organization (Yan et al., 2000; Figure 2A). Most of the UBPs have additionally to their catalytic domain further domains that enable them to interact with different proteins, allowing UBPs to be involved in a broad range of biological processes. However, to date, the molecular functions of UBPs are far from being well resolved in plants, UBP26 being the only member among this family for which the target protein, Histone H2B, is identified (Sridhar et al., 2007).

Bottom Line: One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets.DUBs are also essential for processing ubiquitin precursors and are important for recycling ubiquitin molecules from target proteins prior to their degradation and thereby maintaining the free ubiquitin pool in the cell.Here, we will discuss the five different DUB families (USP/UBP, UCH, JAMM, OTU, and MJD) and their known biochemical and physiological roles in plants.

View Article: PubMed Central - PubMed

Affiliation: Department of Plant Systems Biology, Technische Universität München Freising, Germany.

ABSTRACT
Ubiquitylation is a reversible post-translational modification that is involved in various cellular pathways and that thereby regulates various aspects of plant biology. For a long time, functional studies of ubiquitylation have focused on the function of ubiquitylating enzymes, especially the E3 ligases, rather than deubiquitylating enzymes (DUBs) or ubiquitin isopeptidases, enzymes that hydrolyze ubiquitin chains. One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets. However, recent studies have revealed that DUBs also actively participate in controlling cellular events and thus play pivotal roles in plant development and growth. DUBs are also essential for processing ubiquitin precursors and are important for recycling ubiquitin molecules from target proteins prior to their degradation and thereby maintaining the free ubiquitin pool in the cell. Here, we will discuss the five different DUB families (USP/UBP, UCH, JAMM, OTU, and MJD) and their known biochemical and physiological roles in plants.

No MeSH data available.