Vertebrate GLD2 poly(A) polymerases in the germline and the brain.
Cytoplasmic polyadenylation is important in the control of mRNA stability and translation, and for early animal development and synaptic plasticity. Here, we focus on vertebrate poly(A) polymerases that are members of the recently described GLD2 family. We identify and characterize two closely related GLD2 proteins in Xenopus oocytes, and show that they possess PAP activity in vivo and in vitro and that they bind known polyadenylation factors and mRNAs known to receive poly(A) during development. We propose that at least two distinct polyadenylation complexes exist in Xenopus oocytes, one of which contains GLD2; the other, maskin and Pumilio. GLD2 protein interacts with the polyadenylation factor, CPEB, in a conserved manner. mRNAs that encode GLD2 in mammals are expressed in many tissues. In the brain, mouse, and human GLD2 mRNAs are abundant in anatomical regions necessary for long-term cognitive and emotional learning. In the hippocampus, mouse GLD2 mRNA colocalizes with CPEB1 and Pumilio1 mRNAs, both of which are likely involved in synaptic plasticity. We suggest that mammalian GLD2 poly(A) polymerases are important in synaptic translation, and in polyadenylation throughout the soma.
Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.
Labib
L
Rouhana
Liaoteng
L
Wang
Natascha
N
Buter
Jae Eun
JE
Kwak
Craig A
CA
Schiltz
Tania
T
Gonzalez
Ann E
AE
Kelley
Charles F
CF
Landry
Marvin
M
Wickens
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology* / Q000378:metabolism; D020134:Catalytic Domain; D005260:Female; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D051379:Mice; D008845:Microinjections; D008969:Molecular Sequence Data; D009865:Oocytes / Q000201:enzymology* / Q000378:metabolism; D011062:Polynucleotide Adenylyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D013154:Spleen / Q000166:cytology; D014981:Xenopus; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D039221:mRNA Cleavage and Polyadenylation Factors / Q000378:metabolism
D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D029867:Xenopus Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; D005982:Glutathione Transferase; D011062:Polynucleotide Adenylyltransferase