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M Caizergues-Ferrer

Publications and source records attributed to M Caizergues-Ferrer.

45 records · Page 3Linked to original sources
PubMed1983

Maturation of a 100 kDa protein associated with preribosomes in Chinese hamster ovary cells.

A 100 kDa nucleolar protein which is transitorily associated with preribosomes in the nucleoli of Chinese hamster ovary cells has been found to be specifically cleaved by a thiol protease. During an 'in vitro' incubation of nucleoli, the 100 kDa protein is processed into eight different proteins which are detected by immunoreaction with a serum raised against the 100 kDa protein. Qualitative and quantitative variations in the maturation products of the 100 kDa protein are obtained by 'in vitro' incubation of the 60S and 80S preribosomes. The 100 kDa protein has been purified to homogeneity with the protease activity still associated. The properties of the enzyme are described and its role in the maturation of preribosomes is discussed.

Animals↗
PubMed1982

Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein.

A high-molecular-mass nucleolar protein (100-kDa protein) is associated with nascent pre-rRNA and pre-ribosomes in Chinese hamster ovary cells. We have prepared antiserum against the 100-kDa protein and we have used it to study the intracellular localization and the possible processing of this protein. Serologically related proteins were detected in the nucleolus and in ribosomes. Proteins of various subcellular fractions were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transferred to nitrocellulose filters, reacted with serum and the protein-immunoglobulin complexes were revealed by 125I-labeled protein A. In the nucleolus, four proteins with molecular masses of 100 kDa, 95 kDa, 76 kDa and 70 kDa were thus visualized. In the ribosomes, two proteins (of 100 kDa and 76 kDa) gave a strong reaction while six others (of 70 kDa, 60 kDa, 50 kDa, 30 kDa, 21 kDa, 18 kDa) reacted slightly. By immunological precipitation of total cell extracts, we have shown that the 100-kDa protein antiserum cross-reacts with five proteins with molecular masses of 120 kDa, 100 kDa, 95 kDa, 70 kDa and 60 kDa. Specific degradation of the 100-kDa protein into similar peptides with molecular masses of 95 kDa, 76 kDa, 70 kDa, 60 kDa and 50 kDa can be achieved by incubation of isolated nucleoli or of purified 100-kDa protein in vitro. Cleavage of the protein is due to a thiol endoprotease which is tightly bound to the 100-kDa protein. Possible relations between the maturation of this preribosomal protein into ribosomal proteins and the processing of preribosomal RNA into mature ribosomal RNA are discussed.

Animals↗
PubMed1981

Synthesis and behaviour of small RNA species of CHO cells submitted to a heat chick.

Incubation of Chinese hamster ovary (CHO) cells for 1 hour at 43 degrees C results in an inhibition of high molecular weight RNA synthesis while most of the ow molecular weight RNAs are still synthesized. In cells returned to 37 degrees C, the transcription of high molecular weight RNA is reinitiated after 7 h recovery. The synthesis of snRNA A, C, D which are transcribed by RNA polymerase B (II) is inhibited in cells incubated at 43 degrees C while the synthesis of 4S, 5S, L and K components is not affected. During the recovery period the synthesis of low molecular weight RNA is increased variously according to the components relative to control cells : x 1.5 for 5S RNA to x 8 for snK. After 9 h recovery at 37 degrees C, snA and SnD are again synthesized but newly synthesized snC does not appear in the nucleus while a putative preC component accumulates in the cytoplasm. On the other hand, the distribution of all the pre-existing low molecular weight RNAs is not affected by the heat shock.

Animals↗
PubMed1980

Effects of heat shock on nuclear and nucleolar protein phosphorylation in Chinese hamster ovary cells.

Distribution and 32P labeling of nuclear and nucleolar phosphoproteins were studied in Chinese hamster ovary cells incubated at supranormal temperature (1 h at 43 degrees C). The heat shock induced the phosphorylation of a nucleolar protein with a molecular weight of 95,000. Similarly, in the non-nucleolar fraction of the nucleus, phosphorylation of a 54,000-Mr protein was induced while a protein with a molecular weight of 35,000 was rapidly dephosphorylated. Except for these definite changes, the labeling pattern of proteins that were 32P labeled prior to the heat shock was not affected. During recovery at 37 degrees C, the efficiency of labeling was reduced (10-50% of control values accoring to the subcellular fraction) and certain changes in labeling of phosphoproteins were detected. The nucleolar protein of 95,000 Mr was no longer phosphorylated. Phosphorylation of the 54,000-Mr protein, induced by heat shock, continued during the first 4 h of recovery at 36 degrees C and then stopped. The 35,000-Mr protein was slightly phosphorylated during the first hours at 37 degrees C and progressively reached its control level by 7 h. These findings,along with previous results on the effects of heat shock on RNA synthesis, suggest that the phosphorylation level of the three phosphoproteins may play a role in the regulation of transcription and in RNA processing.

Animals↗
PubMed1979

Effects of heat shock on gene expression and subcellular protein distribution in Chinese hamster ovary cells.

Incubation of Chinese Hamster Ovary (CHO) cells for one hour at 43 degrees C results in several obvious changes in protein distribution and protein synthesis. One major protein of the cytoplasm (molecular weight 45,000 daltions), also present as a minor component in the nucleus, rapidly disappeared while several proteins, especially high molecular weight peptides, were induced by heat shock. Localization of the proteins in the cytoplasm, extra-nucleolar chromatin and nucleolar bodies has been carried out. Different sets of induced proteins appear in each subcellular compartment. Four hours after restoration of the normal temperature, the normal pattern of protein synthesis was observed. The 45,000 dalton protein reappeared first. Relations between structural and functional alterations and changes in protein distribution are suggested.

Animals↗
PubMedDate not supplied

Novel intron-encoded small nucleolar RNAs with long sequence complementarities to mature rRNAs involved in ribosome biogenesis.

Recently, several new snoRNAs encoded in introns of genes coding for ribosomal, ribosome-associated, or nucleolar proteins have been discovered. We are presently studying four of these intronic snoRNAs. Three of them, U20, U21, and U24, are closely related to each other on a structural basis. They are included in genes encoding nucleolin and ribosomal proteins L5 and L7a, respectively, in warm-blooded vertebrates. These three metabolically stable snoRNAs interact with nucleolar protein fibrillarin. In addition, they display common features that make them strikingly related to snoRNA U14. U14 contains two tracts of complementarity to 18S rRNA, which are required for the production of 18S rRNA. U20 displays a 21 nucleotide (nt) long complementarity to 18S rRNA. U21 contains a 13 nt complementarity to an invariant sequence in eukaryotic 28S rRNA. U24 has two separate 12 nt long complementarities to a highly conserved tract of 28S rRNA. Phylogenetic evidences support the fundamental importance of the pairings of these three snoRNAs to pre-rRNA, which could be involved in a control of pre-rRNA folding during preribosome assembly. By transfection of mouse cells, we have also analyzed the processing of U20 and found that the -cis acting signals for its processing from intronic RNA are restricted to the mature snoRNA sequence. Finally, we have documented changes of host genes for these three intronic snoRNAs during the evolution of eukaryotes.

Animals↗