Abstract
The serine/arginine (SR)-rich protein family is phylogenetically conserved and plays significant roles in mRNA maturation, including alternative splicing (AS). In Drosophila, SR protein B52 functions as a splicing activator to regulate AS events in several genes, including the Down syndrome cell adhesion molecule (Dscam). In this study, the B52 gene from Litopenaeus vannamei (LvB52) was isolated and characterized. The open reading frame of LvB52 contains 1149 bp encoding 382 amino acids. The deduced LvB52 protein includes two RNA recognition motifs (RRM) at the N terminus and an arginine/serine rich domain (RS rich domain) at the C terminus, and thus shows the expected RRM1-RRM2-RS domain architecture. Tissue tropism analysis revealed that LvB52 is expressed in most tissues and at high levels in stomach and muscle. After white spot syndrome virus (WSSV) infection, a parallel increase in the expression of total LvDscam, tail-less LvDscam, membrane-bound LvDscam and LvB52 was observed after 24 hpi. Conversely, there was no obvious change in the expression of the AS repressor Lvhrp36. In vivo dsRNA silencing of LvB52 induced element 3 exclusion in the LvDscam cytoplasmic tail, but no abnormal exclusions in the Ig2-Ig3 region or the transmembrane region. We also found that the exon of the Ig7 region was quite often excluded, even in normal shrimp, and that LvB52 silencing was associated with a decrease in the variability of this region. Taken together, our data suggest that LvB52 acts as a splicing activator that regulates AS events in LvDscam.
| Original language | English |
|---|---|
| Pages (from-to) | 209-219 |
| Number of pages | 11 |
| Journal | Fish and Shellfish Immunology |
| Volume | 34 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2013 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Environmental Chemistry
- Aquatic Science
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Shrimp Dscam and its cytoplasmic tail splicing activator serine/arginine (SR)-rich protein B52 were both induced after white spot syndrome virus challenge. / Chiang, Yi An; Hung, Hsin Yi; Lee, Chung Wei; Huang, Yun Tzu; Wang, Han-Ching.
In: Fish and Shellfish Immunology, Vol. 34, No. 1, 01.01.2013, p. 209-219.Research output: Contribution to journal › Article
TY - JOUR
T1 - Shrimp Dscam and its cytoplasmic tail splicing activator serine/arginine (SR)-rich protein B52 were both induced after white spot syndrome virus challenge
AU - Chiang, Yi An
AU - Hung, Hsin Yi
AU - Lee, Chung Wei
AU - Huang, Yun Tzu
AU - Wang, Han-Ching
PY - 2013/1/1
Y1 - 2013/1/1
N2 - The serine/arginine (SR)-rich protein family is phylogenetically conserved and plays significant roles in mRNA maturation, including alternative splicing (AS). In Drosophila, SR protein B52 functions as a splicing activator to regulate AS events in several genes, including the Down syndrome cell adhesion molecule (Dscam). In this study, the B52 gene from Litopenaeus vannamei (LvB52) was isolated and characterized. The open reading frame of LvB52 contains 1149 bp encoding 382 amino acids. The deduced LvB52 protein includes two RNA recognition motifs (RRM) at the N terminus and an arginine/serine rich domain (RS rich domain) at the C terminus, and thus shows the expected RRM1-RRM2-RS domain architecture. Tissue tropism analysis revealed that LvB52 is expressed in most tissues and at high levels in stomach and muscle. After white spot syndrome virus (WSSV) infection, a parallel increase in the expression of total LvDscam, tail-less LvDscam, membrane-bound LvDscam and LvB52 was observed after 24 hpi. Conversely, there was no obvious change in the expression of the AS repressor Lvhrp36. In vivo dsRNA silencing of LvB52 induced element 3 exclusion in the LvDscam cytoplasmic tail, but no abnormal exclusions in the Ig2-Ig3 region or the transmembrane region. We also found that the exon of the Ig7 region was quite often excluded, even in normal shrimp, and that LvB52 silencing was associated with a decrease in the variability of this region. Taken together, our data suggest that LvB52 acts as a splicing activator that regulates AS events in LvDscam.
AB - The serine/arginine (SR)-rich protein family is phylogenetically conserved and plays significant roles in mRNA maturation, including alternative splicing (AS). In Drosophila, SR protein B52 functions as a splicing activator to regulate AS events in several genes, including the Down syndrome cell adhesion molecule (Dscam). In this study, the B52 gene from Litopenaeus vannamei (LvB52) was isolated and characterized. The open reading frame of LvB52 contains 1149 bp encoding 382 amino acids. The deduced LvB52 protein includes two RNA recognition motifs (RRM) at the N terminus and an arginine/serine rich domain (RS rich domain) at the C terminus, and thus shows the expected RRM1-RRM2-RS domain architecture. Tissue tropism analysis revealed that LvB52 is expressed in most tissues and at high levels in stomach and muscle. After white spot syndrome virus (WSSV) infection, a parallel increase in the expression of total LvDscam, tail-less LvDscam, membrane-bound LvDscam and LvB52 was observed after 24 hpi. Conversely, there was no obvious change in the expression of the AS repressor Lvhrp36. In vivo dsRNA silencing of LvB52 induced element 3 exclusion in the LvDscam cytoplasmic tail, but no abnormal exclusions in the Ig2-Ig3 region or the transmembrane region. We also found that the exon of the Ig7 region was quite often excluded, even in normal shrimp, and that LvB52 silencing was associated with a decrease in the variability of this region. Taken together, our data suggest that LvB52 acts as a splicing activator that regulates AS events in LvDscam.
UR - http://www.scopus.com/inward/record.url?scp=84871622698&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84871622698&partnerID=8YFLogxK
U2 - 10.1016/j.fsi.2012.10.021
DO - 10.1016/j.fsi.2012.10.021
M3 - Article
VL - 34
SP - 209
EP - 219
JO - Fish and Shellfish Immunology
JF - Fish and Shellfish Immunology
SN - 1050-4648
IS - 1
ER -