Additional file 1: of Origin and development of oligoadenylate synthetase immune system

Text S1. Two transcripts of ostrich OAS1. Table S1. Primers used for real time quantitative RT-PCR. Table S2. Information on OAS structures. Table S3. Distribution of avian OAS genes. Table S4. Energy change of OAS domains after docking with dsRNA. Table S5. Positive selection analysis of the OASL subfamily. Figure S1. 2-5A downregulated the expression of TOP I gene. Cells were transfected with 2-5A in different concentration. TOP I was detected at 6 h post transfection. (a) HeLa cells. (b) DF1 cells. Figure S2. Predicted structure of human OAS2 protein. N terminus (left) and C terminus (right) of OAS2 were colored in red and green respectively. Figure S3. Distribution of positively selected sites for the OASL gene. Sequence alignment was carried out using the PRANK software (version 140,603) and positively selected sites were predicted using PAML software (version 4.9). Sites displaying significant ω values were shown. Sequences for avian OASL, mammalian OASL1 and OASL2 refer to ostrich OASL, alpaca OASL1 and shrew OASL2, respectively. Figure S4. Evolutionary rate of mammalian OASL2 and avian OASL genes. Sequence alignment was performed by PRANK software (version 140,603) and evolutionary rate was calculated using BEAST software (version 2.47). (a) Mammalian OASL2. (b) Avian OASL. It is clear that mammalian OASL2 has evolved faster than avian OASL. Figure S5. Isoelectric point of residues in two UBL domains of OASLs (C terminus of OASL protein; ~ 150 residues). (a-c) Reptilian and avian UBL domains. Common garter snake, duck and chicken OASLs were selected as reptilian and avian OASL representatives. (d-e) Mammalian UBL domains. Mouse and rat OASL2 were selected to represent mammalian OASL2. Avian and reptilian OASL proteins contain more basic residues (pink box) in the second UBL domain, while mammalian OASL proteins prefer to harbor basic residues (pink box) in the first UBL domain. (DOCX 2920 kb