Subcellular localization and interactions among rubber particle proteins from Hevea brasiliensis

Brown, Daniel G.; Feeney, Mistianne; Ahmadi, Mathin; Lonoce, Chiara; Sajari, Roslinda; Cola, Alessandra Di; Frigerio, Lorenzo

doi:10.1093/jxb/erx331

Cited by 46 publications

(45 citation statements)

References 26 publications

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“…Yamashita et al (2016) reported that a protein complex, consisting of HRT1, REF, and HRT1-REF BRIDGING PROTEIN in the ER, constitutes the biosynthetic machinery for natural rubber. It is known that in H. brasiliensis rubber particles originate from the ER (Shi et al, 2016), which was further confirmed by Brown et al (2017). Together, we concluded that Eu-rubber biosynthesis could occur in the ER also.…”

Section: Discussionsupporting

confidence: 82%

The Hardy Rubber Tree Genome Provides Insights into the Evolution of Polyisoprene Biosynthesis

et al. 2018

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Eucommia ulmoides, also called hardy rubber tree, is an economically important tree; however, the lack of its genome sequence restricts the fundamental biological research and applied studies of this plant species. Here, we present a high-quality assembly of its ∼1.2-Gb genome (scaffold N50 = 1.88 Mb) with at least 26 723 predicted genes for E. ulmoides, the first sequenced genome of the order Garryales, which was obtained using an integrated strategy combining Illumina sequencing, PacBio sequencing, and BioNano mapping. As a sister taxon to lamiids and campanulids, E. ulmoides underwent an ancient genome triplication shared by core eudicots but no further whole-genome duplication in the last ∼125 million years. E. ulmoides exhibits high expression levels and/or gene number expansion for multiple genes involved in stress responses and the biosynthesis of secondary metabolites, which may account for its considerable environmental adaptability. In contrast to the rubber tree (Hevea brasiliensis), which produces cis-polyisoprene, E. ulmoides has evolved to synthesize long-chain trans-polyisoprene via farnesyl diphosphate synthases (FPSs). Moreover, FPS and rubber elongation factor/small rubber particle protein gene families were expanded independently from the H. brasiliensis lineage. These results provide new insights into the biology of E. ulmoides and the origin of polyisoprene biosynthesis.

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Section: Discussionsupporting

confidence: 82%

The Hardy Rubber Tree Genome Provides Insights into the Evolution of Polyisoprene Biosynthesis

et al. 2018

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“…Even so, the presence of helix 8 is unique and its function is worth further investigation. A possibility might be association with cell membrane or membrane-bound anchoring proteins, because AbUPPS lacks the extended N-terminus as observed, for example, in rubber synthase (Brown et al, 2017).…”

Section: Discussionmentioning

confidence: 99%

Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii

Huang

Lai

et al. 2018

Acta Crystallogr F Struct Biol Commun

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Undecaprenyl pyrophosphate (UPP) is an important carrier of the oligosaccharide component in peptidoglycan synthesis. Inhibition of UPP synthase (UPPS) may be an effective strategy in combating the pathogen Acinetobacter baumannii, which has evolved to be multidrug-resistant. Here, A. baumannii UPPS (AbUPPS) was cloned, expressed, purified and crystallized, and its structure was determined by X-ray diffraction. Each chain of the dimeric protein folds into a central -sheet with several surrounding -helices, including one at the C-terminus. In the active site, two molecules of citrate interact with the side chains of the catalytic aspartate and serine. These observations may provide a structural basis for inhibitor design against AbUPPS.

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“…In addition, it also has many other functions, such as calcium homeostasis (Hong et al ., 1999), oil and protein body formation (Huang, 1996; Herman, 2008), rubber particle formation (Brown et al ., 2017) and auxin regulation (Friml & Jones, 2010; Kriechbaumer et al ., 2015). …”

Section: Introductionmentioning

confidence: 99%

“…As the first biosynthetic organelle in the plant secretory pathway, the endoplasmic reticulum (ER) underpins the production, folding and quality control of proteins (Brandizzi et al, 2003;Hawes et al, 2015), as well as lipid biosynthesis (Wallis & Browse, 2010). In addition, it also has many other functions, such as calcium homeostasis (Hong et al, 1999), oil and protein body formation (Huang, 1996;Herman, 2008), rubber particle formation (Brown et al, 2017) and auxin regulation (Friml & Jones, 2010;Kriechbaumer et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis Lunapark proteins are involved in ER cisternae formation

et al. 2018

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Summary The plant endoplasmic reticulum (ER) is crucial to the maintenance of cellular homeostasis. The ER consists of a dynamic and continuously remodelling network of tubules and cisternae. Several conserved membrane proteins have been implicated in formation and maintenance of the ER network in plants, such as RHD3 and the reticulon proteins. Despite the recent work in mammalian and yeast cells, the detailed molecular mechanisms of ER network organization in plants remain largely unknown. Recently, novel ER network‐shaping proteins called Lunapark (LNP) have been identified in yeast and mammalian cells.Here we identify two Arabidopsis LNP homologues and investigate their subcellular localization via confocal microscopy and potential function in shaping the ER network using protein–protein interaction assays and mutant analysis.We show that AtLNP1 overexpression in tobacco leaf epidermal cells mainly labels cisternae in the ER network, whereas AtLNP2 labels the whole ER. Overexpression of LNP proteins results in an increased abundance of ER cisternae and lnp1 and lnp1lnp2 amiRNA lines display a reduction in cisternae and larger polygonal areas.Thus, we hypothesize that AtLNP1 and AtLNP2 are involved in determining the network morphology of the plant ER, possibly by regulating the formation of ER cisternae.

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Subcellular localization and interactions among rubber particle proteins from Hevea brasiliensis

Abstract: The major proteins of rubber particles from Hevea brasiliensis associate with the endoplasmic reticulum membrane and can interact with the key cytosolic biosynthetic enzyme cis-prenyltransferase.

Cited by 46 publications

References 26 publications

The Hardy Rubber Tree Genome Provides Insights into the Evolution of Polyisoprene Biosynthesis

The Hardy Rubber Tree Genome Provides Insights into the Evolution of Polyisoprene Biosynthesis

Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii

Arabidopsis Lunapark proteins are involved in ER cisternae formation

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