Maternal Paracentrotus lividus RNAs are differentially localized during the first cell division.
In Paracentrotus lividus eggs, there are RNAs localized at the animal and vegetal poles. During the first cell division, some of these RNAs are associated with the mitotic spindle, whereas others are free in the cytoplasm. Among the RNAs bound to mitotic apparatus (MA), we have found the mitochondrial 16S rRNA. By immunohistochemistry we have also detected hsp60, a mitochondrial membrane protein, localized around the MA, suggesting that the entire mitochondria are associated with it. Western blotting of proteins prepared by cellular fractionation after detergent treatment of P. lividus eggs revealed that both hsp60 and cytochrome c are not associated with cytoskeletal elements. All the above data have been confirmed by immunoblot analyses of preparations of microtubules and MA in which the presence of hsp60 and cytochrome c were detected only in the MA fraction. Moreover, mitochondrial succinate dehydrogenase activity was determined in MA and cytoplasm fractions during the first cell division, and the localization and vitality of the organelles were also confirmed by in vivo staining with Mito red. A possible role for mitochondria in the asymmetric distribution of RNAs and in cell division is discussed.
Istituto di Biologia ed Immunologia Molecolare Alberto Monroy CNR, via Ugo La Malfa 153, 90146 Palermo, Italy.
Daniele P
DP
Romancino
Giovanna
G
Montana
Marta
M
Di Carlo
D000818:Animals; D002455:Cell Division; D018834:Chaperonin 60 / Q000378:metabolism; D045304:Cytochromes c / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D008928:Mitochondria / Q000201:enzymology; D012336:RNA, Ribosomal, 16S / Q000235:genetics / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012617:Sea Urchins / Q000166:cytology / Q000235:genetics*; D013385:Succinate Dehydrogenase / Q000378:metabolism
D018834:Chaperonin 60; D012336:RNA, Ribosomal, 16S; D045304:Cytochromes c; D013385:Succinate Dehydrogenase