The ribosomal protein L32-2 (RPL32-2) of S. pombe exhibits a novel extraribosomal function by acting as a potential transcriptional regulator.
Ribosomal proteins play important roles in stabilizing the rRNA structure to facilitate protein synthesis in ribosome. In the present study, we analyzed the potential extraribosomal function of the ribosomal protein L32-2 (RPL32-2), which was expressed by a gene clone isolated from a cDNA library of Schizosaccharomyces pombe (S. pombe). RPL32-2 fused with the GAL4 DNA-bind domain or the GAL4 transcriptional activating domain could, respectively, activate transcriptions of reporter genes in yeast strain AH109. The RPL32-2 mutants with truncation of either the N- or the C-terminal domain resulted in abolishment of this regulatory effect. The DNA binding site for RPL32-2 of S. pombe was identified by using a random oligonucleotide selection strategy and gel motility shift assay and Western blotting confirmed its binding specificity. Moreover, we found RPL32-2 was also able to interact with a to-be-identified AT sequence binding protein. These data suggest that RPL32-2 of S. pombe, besides its ribosomal function, may also act as a potential transcriptional regulator in nucleus.
Wang
Jing
J
Jiangsu Key Lab for Biodiversity and Biotechnology, NNU Key Lab of Microbial Technology, College of Life Science, Nanjing Normal University, 122 Ninghai Lu, Nanjing 210097, PR China.
Jing
Wang
W
Yuan
Sheng
S
Sheng
Yuan
Y
Jiang
Shibo
S
Jang
Shibo
S
D001665:Binding Sites; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D012269:Ribosomal Proteins / Q000502:physiology*; D012568:Schizosaccharomyces / Q000737:chemistry / Q000235:genetics*; D029702:Schizosaccharomyces pombe Proteins / Q000502:physiology*; D014157:Transcription Factors; D015533:Transcriptional Activation
D009687:Nuclear Proteins; C510544:RPL32-2 protein, S pombe; D011993:Recombinant Fusion Proteins; D012269:Ribosomal Proteins; D029702:Schizosaccharomyces pombe Proteins; D014157:Transcription Factors