In construction

Tunicate cellulose has potential applications, such as the synthesis of weavable fibers for wearable sensors (Cho and coll., 2019).

CesA from C savignyi can rescue A. tumefaciens mutants (Matthysse and coll., 2004).

Sasakura and coll. (2016) have proposed that the GC-rich genome of actinobacteria might have provided an AP-2 binding site promoting expression in the epidermis.

A cellulose synthase and several endoglycanase genes were observed in the C. intestinalis genome by Dehal and coll., 2002.

CesA is not found in other animals outside Tunicates. The GH6 (cellulose hydrolase) gene is found as an independent copy and as a domain of CesA in Tunicates (Inoue, Nakashima and Satoh, 2019). In Oikopleura, GHC6-1 lacks a conserved catalytic aspartate (Li and coll., 2020).

In Oikopleura, the structure of cellulose fibers is triclinic I(α) in larval stages and monoclinic I(β) in the house. This correlates with the expression of Od-CesA1 and Od-CesA2 respectively. (Sagane and coll., 2010, Nakashima and coll., 2011). The expression of Od-CesA2 might be cyclic (Nakashima and coll., 2011).

The house of O. rufescens is also made of cellulose Iβ (Kimura and coll., 2001).

Chitin-based barrier immunity and its loss predated mucus-colonization by indigenous gut microbiota.

Nakashima K, Kimura S, Ogawa Y, Watanabe S, Soma S, Kaneko T, Yamada L, Sawada H, Tung CH, Lu TM, Yu JK, Villar-Briones A, Kikuchi S, Satoh N.

Nat Commun. 2018 Aug 24;9(1):3402. doi:10.1038/s41467-018-05884-0

Chitin-based barrier immunity and its loss predated mucus-colonization by indigenous gut microbiota.

The gut cells of Ciona robusta are protected by a membrane made of cellulose and chitin, that bacteria can not cross. The three most abundant proteins in this membrane are Ci-MACPF1, related to perforins, variable region-containing chitin-binding protein (VCBP), and Ci-GFM1, a gel-forming mucin. Thus, the tunicate gut has features related to insects (chitin barrier) and vertebrates (mucin barrier).

Phylogenetic Analyses of Glycosyl Hydrolase Family 6 Genes in Tunicates: Possible Horizontal Transfer.

Li KL, Nakashima K, Inoue J, Satoh N.

Genes (Basel). 2020 Aug 13;11(8):937. doi:10.3390/genes11080937

Phylogenetic Analyses of Glycosyl Hydrolase Family 6 Genes in Tunicates: Possible Horizontal Transfer.

Comparison of primary sequence and of intron position suggests that GHC6-1 was transferred in a common ancestor of all living tunicates. O. dioica's GH6-1 gene lacks a conserved catalytic aspartate, and does not share introns with the other tunicate genes.

“We found that in many tunicate GH6-1 proteins, an aspartic acid can be aligned to the catalytic H. jecorina D221, except for SthGH6-1b (E197) and OdiGH6-1 (K211). However, the catalytic aspartic acid was not conserved in tunicate CesA.”

“In this study, although we found no other sites shared between genes of O. dioica and other tunicates, we found that many shared splice sites are present among GH6-containing genes from three other major clades of tunicates (Thaliacea + Phlebobranchia + Stolidobranchia). It is reasonable to assume that many shared introns were acquired after the branching of larvaceans and before the subsequent divergence of major tunicate clades.”

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The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins.

Dehal P, Satou Y, Campbell RK, Chapman J, Degnan B, De Tomaso A, Davidson B, Di Gregorio A, Gelpke M, Goodstein DM, Harafuji N, Hastings KE, Ho I, Hotta K, Huang W, Kawashima T, Lemaire P, Martinez D, Meinertzhagen IA, Necula S, Nonaka M, Putnam N, Rash S, Saiga H, Satake M, Terry A, Yamada L, Wang HG, Awazu S, Azumi K, Boore J, Branno M, Chin-Bow S, DeSantis R, Doyle S, Francino P, Keys DN, Haga S, Hayashi H, Hino K, Imai KS, Inaba K, Kano S, Kobayashi K, Kobayashi M, Lee BI, Makabe KW, Manohar C, Matassi G, Medina M, Mochizuki Y, Mount S, Morishita T, Miura S, Nakayama A, Nishizaka S, Nomoto H, Ohta F, Oishi K, Rigoutsos I, Sano M, Sasaki A, Sasakura Y, Shoguchi E, Shin-i T, Spagnuolo A, Stainier D, Suzuki MM, Tassy O, Takatori N, Tokuoka M, Yagi K, Yoshizaki F, Wada S, Zhang C, Hyatt PD, Larimer F, Detter C, Doggett N, Glavina T, Hawkins T, Richardson P, Lucas S, Kohara Y, Levine M, Satoh N, Rokhsar DS.

Science. 2002 Dec 13;298(5601):2157-67 doi: 10.1126/science.1080049

The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins.

The genome of C. intestinalis contains at least one cellulose synthans and multiple endoglycanases.

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Transcriptional regulation of a horizontally transferred gene from bacterium to chordate.

Sasakura Y, Ogura Y, Treen N, Yokomori R, Park SJ, Nakai K, Saiga H, Sakuma T, Yamamoto T, Fujiwara S, Yoshida K.

Proc Biol Sci. 2016 Dec 28;283(1845). pii: 20161712. doi:10.1098/rspb.2016.1712

Transcriptional regulation of a horizontally transferred gene from bacterium to chordate.

GC-rich DNA from Actinobacteria contains AP-2 binding sites, which triggers expression in the epidermis. This might have facilitated horizontal transfer of the CesA gene.

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The evolutionary origin of animal cellulose synthase.

Nakashima K, Yamada L, Satou Y, Azuma J, Satoh N.

Dev Genes Evol. 2004 Feb;214(2):81-8.

The evolutionary origin of animal cellulose synthase.

The cellulose synthase genes in Tunicates are thought to be of actinobacterial origin, because the tunicate CesA gene contains two domains with similarity with a cellulose synthase and a cellulase of the glycoside hydrolase (GH)-6 family, and these genes are often found in proximity in actinobacteria.

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The evolving proteome of a complex extracellular matrix, the Oikopleura house.

PLoS One. 2012;7(7):e40172. doi:10.1371/journal.pone.0040172

Hosp J, Sagane Y, Danks G, Thompson EM.

The evolving proteome of a complex extracellular matrix, the Oikopleura house.

“Almost half of the oikosin complement exhibit no known domain structures or other similarities to known proteins, suggesting de novo appearance in the appendicularian lineage. Known domains are implicated in cellulose binding, protein-protein interactions or sPLA2 activity. Production of the latter is concentrated in epithelial regions associated with construction of the fcf, suggesting a possible role of this structure in innate immune defence.” “The genomic organization of oikosin loci appears incompatible with common enhancers or locus control regions exerting [...] a coordinate regulatory role.”

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