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Biomedical subjects

D Henning

Publications and source records attributed to D Henning.

At least 73 records · Page 4Linked to original sources
PubMed1983

Identification of a La protein binding site in a RNA polymerase III transcript (4.5 I RNA).

Anti-La antibodies are frequently found in patients with autoimmune diseases; the antigen was reported to be a 50,000-Da protein (Rinke, J., and Steitz, J. A. (1982) Cell 29, 149-159). Because this protein was associated with many nascent RNA polymerase III transcripts, it was suggested to be an RNA polymerase III transcription factor. The present study was designed to analyze 4.5 I ribonucleoprotein, an RNA polymerase III transcript which contains the La antigen. It was found that the 3'-end 20-30-nucleotide portion was the most protected portion of 4.5 I RNA when 4.5 I ribonucleoprotein was digested with T1 RNase. When U2 RNA (an RNA polymerase II transcript) and 4.5 I RNA were incubated with the S-100 fraction of Novikoff hepatoma cells, the 4.5 I RNA bound La antigen but the U2 RNA did not. When partial and complete T1 RNase digestion fragments of 4.5 I RNA were incubated with the S-100 fraction, the 3'-end fragments bound preferentially to the La antigen. However, the fragments of 4.5 I RNA bound less efficiently to La antigen than whole 4.5 I RNA. These results indicate that the 3'-end of 4.5 I RNA is the La antigen binding site in this molecule and suggest that the overall conformation of RNA aids in the binding of La antigen.

Animals↗
PubMed1983

Detection of a nucleolar 7-2 ribonucleoprotein and a cytoplasmic 8-2 ribonucleoprotein with autoantibodies from patients with scleroderma.

In studies on antinucleolar antibodies in sera from 24 patients with scleroderma, an autoimmune disease, one serum, designated "anti-To", contained antibodies against a nucleolar 7-2 ribonucleoprotein and a novel cytoplasmic 8-2 ribonucleoprotein. The 7-2 and 8-2 RNAs are distinct RNAs with a pppG terminus. They are partially conserved between rat and human species and are present in distinct ribonucleoprotein particles. Eight sera contained antibodies that precipitated particles containing nucleolar U3 RNA; these antibodies appear to be directed against preribosomal particles containing U3 ribonucleoprotein, rather than the U3 ribonucleoprotein particles alone. All these ribonucleoproteins required proteins for antigenicity. These antibodies will be of use in studies on the structure and function of these novel small ribonucleoproteins.

Animals↗
PubMed1983

The nucleotide sequence of 8 S RNA bound to preribosomal RNA of Novikoff hepatoma. The 5'-end of 8 S RNA is 5.8 S RNA.

8 S RNA of Novikoff hepatoma was characterized by fingerprinting, sequencing gels, and by hybridization to rat ribosomal DNA clones. The data obtained show that 8 S RNA is 273 or 274 nucleotides long; ribosomal 5.8 S RNA is its 5'-terminal 156 nucleotides. All the post-transcriptional modifications found in 5.8 S rRNA were also found in 8 S RNA; no other modifications were found. The 3'-terminal 118 nucleotides were consistent with the adjoining internal transcribed spacer sequence in rDNA (Subrahmanyam, C. S., Cassidy, B., Busch, H., and Rothblum, L. (1982) Nucleic Acids Res. 10, 3667-3680). Based on its nucleolar localization, the finding that all the 8 S RNA is hydrogen-bonded to preribosomal RNA and its consistency in sequence to the cloned rat ribosomal DNA sequence, it appears that 8 S RNA is a relatively stable intermediate in the formation of 5.8 S rRNA from 45 S pre-rRNA. This stable intermediate RNA may be a useful substrate for studies on rRNA processing and for studies on eukaryotic rRNA-processing enzyme(s).

Animals↗
PubMed1982

Nucleotide sequence of 7 S RNA. Homology to Alu DNA and La 4.5 S RNA.

7 S RNA, a component of normal higher eukaryotic cells and several oncornaviruses, was shown to be conserved in evolution (Erikson, E., Erikson, R. L., Henry, B., and Pace, N. R. (1973) Virology 53, 40-46). Recently, 7 S RNA was shown to be partially complementary to Alu family DNA sequences (Weiner, A. (1980) Cell 22, 209-218). In the present study the nucleotide sequence of Novikoff hepatoma 7 S RNA was determined to be: (formula, see text) Comparison of 7 S RNA, Alu and B1 family DNA, and La 4.5 S RNA sequences for homologies showed that 1) one-third of 7 S RNA, mainly the 5'-end, was homologous to Alu and B1 family sequences; 2) one 300-nucleotide long Alu family sequence contained two binding sites for 7 S RNA; and 3) the 5'-ends of 7 S RNA and La 4.5 S RNA also had extensive (60%) homologies. A model for the secondary structure of 7 S RNA based on maximal base pairing and preferential nuclease cleavage sites is also presented.

Animals↗
PubMed1981

Primary and secondary structure of U2 snRNA.

With the improved rapid sequencing techniques, the earlier sequence of U2 RNA of Novikoff hepatoma (Shibata et al, J. Biol. Chem. 250, 3909-3920, 1975) was reanalyzed and modified. The improved sequence of U2 RNA is 188 (or 189) nucleotides long and is in register with a characterized U2 RNA pseudogene (Denison et al, PNAS 78, 810-814, 1981) except for an 11 nucleotide sequence (nucleotides 147-157) which is absent from the pseudogene. From these results, a secondary structure of U2 RNA is proposed which is supported by the preferred cleavage sites with T1-RNase, RNase A and S1 nuclease. Isolated U2 RNA was cleaved by T1-RNase preferentially at positions 64 and 164, whereas U2 RNA in U2-snRNP was cleaved only at position 64, indicating that position 164 is protected in U2-snRNP. As with U1 RNA (Epstein et al, PNAS 78, 1562-1566, 1981) the 5'-end of isolated U2 RNA was not preferentially cleaved by T1-RNase.

Animals↗
PubMed1981

The primary nucleotide sequence of U4 RNA.

U4 RNA is one of the "capped" nuclear snRNAs recently found to be precipitable by anti-Sm antibodies as ribonucleoprotein particles. U4 RNA, along with other snRNAs, has been implicated in hnRNA processing, mRNA transport, or both (Lerner, M. R., Boyle, J., Mount, S., Wolin, S., and Steitz, J. A. (1980) Nature 283, 220-224). Since the proteins bound to different snRNAs appear to be the same, the functions of different snRNPs might be dependent on the RNA components. To help understand the function of U4 RNP, the nucleotide sequence of U4 RNA was determined. The sequence is (formula see text) In addition to the modified nucleotides in the "cap," U4 RNA contains Am at position 63 and m6A at position 98. It also exhibited A-C microheterogeneity at position 97.

Animals↗
PubMed1980

The nucleotide sequence of nuclear U6 (4.7 S) RNA.

The low molecular weight RNA species which have been purified and characterized in this laboratory (T.S. Ro-Choi and H. Busch (1974) in The Cell Nucleus, Vol. 3, pp 151-208; Academic Press, New York) are now of interest because of their suggested role in processing of heterogeneous nuclear RNAs (Lerner, M.R., Boyle, J.A., Mount, S.M., Wolin, S.L., and Steitz, J.A. (1980) Nature, 283, 220-224). A previously uncharacterized RNA, U6 (4.7 S) nuclear RNA, which is 106 nucleotides long, was extracted from Novikoff hepatoma ascites cell nuclei and purified by polyacrylamide gel electrophoresis. The primary nucleitde sequence of U6 RNA was determined by subjecting the RNA to several types of enzymatic digestions and gel-sequencing techniques. The sequence is: (formula: see text). U6 RNA contains three pseudouridylic acid residues, four alkali-stable dinucleotides, two alkali-stable trinucleotides, one m6adenosine, and one m2guanosine and is notable for the high concentration of modified nucleotides in the center of the molecule. U6 RNA has an unusual 5' terminus which has not yet been fully characterized.

Animals↗
PubMed1980

Substitutions, insertions, and deletions in two highly conserved U3 RNA species.

In view of the increasing interest in low molecular weight ribonucleoprotein particles in exon-intron binding and cleavage reactions (Lerner, M. R., Boyle, J. A., Mount, S. M., Wolin, S. L., and Steitz, J. A. (1980) Nature 283, 220--224), the complementarity of the conserved regions to HnRNAs, or protein binding sites, or both, is of potential importance. U3A, U3B, and U3C are three RNA species localized to the nucleolus of Novikoff hepatoma cells. The nucleotide sequence of U3A RNA determined in this study was compared to that of U3B RNA (Reddy, R., Henning, D., and Busch, H. (1979) J. Biol. Chem. 254, 11097--11105). Both U3A and U3B RNAs contained 5' "caps" and were 216 nucleotides long. The nucleotide sequence 1 to 87 was identical in both U3A and U3B, but differences were found at 18 positions in the remainder of the sequence. Of these differences, 11 were single base replacements, two were dinucleotide replacement AU leads to GG at positions 93 to 94, UC leads to GG at positions 173 to 174, and one was a trinucleotide replacement, UCG leads to CUU at positions 179 to 181. Of the total 18 base replacements, 11 (61%) were purine leads to purine or pyrimidine leads to pyrimidine. Interestingly, two base insertions/deletions were found in each RNA when both RNA sequences were compared for maximum sequence similarity. These data establish that the heterogeneity of some low molecular weight nuclear and nucleolar RNA species resulted from a small number of mutations but much of the sequence was conserved.

Animals↗
PubMed1979

Nucleotide sequence of nucleolar U3B RNA.

U3A, U3B, and U3C are three distinct molecular weight nucleolar RNAs present in Novikoff hepatoma ascites cells. The primary nucleotide sequence of U3B, the most prominent of these U3 species, was determined. Purified U3B RNA was subjected to various enzymatic digestion procedures, including digests of 32P-labeled U3B RNA, RNA ligase, and polynucleotide kinase labeling, for determination of its primary sequence which is: (formula: see text). The 5'-terminus of the RNA has a "cap" and localized purine-rich regions were found near the 3'-terminus, which have been incorporated into a hydrogen-bonded region in a proposed secondary structure of the molecule.

Animals↗
PubMed1975

The primary nucleotide sequence of nuclear U-2 ribonucleic acid. The 5'-terminal portion of the molecule.

The nuclear U-2 RNA which is highly modified (Reddy, R., Ro Choi, T.S., Henning, D., Shibata, H., Choi, Y.C., and Busch H. (1972) J. Biol. Chem. 247, 7245-7250) contains 13 pseudouridylic acid residues, 10 2'-O-methylated nucleotides and two modified bases including N-2,2, 7-trimethyl guanylic acid in its 5'-terminal portion (69 nucleotides). With the determination of this sequence and its overlap with the 3' portion of the molecule (nucleotides 70 to 196), the over-all nucleotide sequence of this RNA is:(see article). The concentration of modified nucleotides in its 5' portion is greater than for any RNA sequenced thus far.

Base Sequence↗
PubMed1975

Nucleotide sequence of U-2 ribonucleic acid. The sequence of the 5'-terminal oligonucleotide.

The nucleotide sequences were determined for the 5'-oligonucleotides obtained by complete pancreatic RNase digestion (P25) and complete T1 RNase digestion (T27) of U-2 RNA. Complete digestion of oligonucleotide P25 with snake venom phosphodiesterase produced pm3 2,2,7G, pAm, pUm, and pCp in approximately equimolar ratios. Partial digestion of these oligonucleotides with snake venom phosphodiesterase produced -Um-C-Gp and pAm-Um, indicating the sequence of the 3'-terminal portion of the 5'-oligonucleotide is pAm-Um-C-Gp. The 5'-terminal oligonucleotide did not contain a 5'-phosphate and no free nucleoside was released from the 5' end by venom phosphodiesterase digestion. Since free pm3 2,2,7G was released by digestion with nucleotide pyrophosphatase and limited digestion with snake venom phosphodiesterase, this nucleotide is apparently linked to pAm in a pyrophosphate linkage. Mass spectrometry and thin layer chromatography in borate systems showed the ribose of m3 2, 2, 7G contains no 2'O-methyl residue. Moreover, the finding that the ribose of m3 2, 2, 7G was oxidized by NaIO4 and reduced by KB3H4 in intact U-2 RNA rules out other linkages involving the 2' and 3' positions. Accordingly, it is concluded that the structure of the 5'-terminal pentanucleotide of U-2 RNA is(see article).

Alkaline Phosphatase↗