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E Ungewickell

Publications and source records attributed to E Ungewickell.

51 records · Page 3Linked to original sources
PubMed1980

The topography of the 5' end of 16-S RNA in the presence and absence of ribosomal proteins S4 and S20.

A ribonucleoprotein prepared by strong ribonuclease digestion of a complex of 16-S ribosomal RNA and proteins S4 and S20 from Escherichia coli has been characterized; its nucleotide sequence, the positions of enzyme cuts and the sequence excisions have been placed in the completed sequence of 16-S RNA. The positions and yields of enzyme cuts, and excisions of sequence, are compared with those of various ribonucleoproteins prepared with S4 or S20 alone, and with the ribonuclease-resistant S4 RNA prepared from renatured 16-s RNA in the absence of ribosomal protein. These data yield important information on the topography and organisation of the 5' third of the 16-s RNA which is selectively maintained in its native conformation by the bound proteins; they also provide criteria for testing secondary structural models of this region of 16-S RNA.

Base Sequence↗
PubMed1980

A conformational study of human spectrin.

Urea denaturation profiles of spectrin dimer, measured by circular dichroism in the regions of the peptide and aromatic Cotton effects, reflect the existence of several independently unfolding domains, as well as the presence of flexible, non-globular structure. As shown by sedimentation velocity and cross-linking experiments, dissociation of the two subunits largely precedes unfolding. The flexible, segmentally mobile structure reveals itself further in the appearance of sharp signals in the high-resolution proton magnetic resonance spectrum. These spectra reveal that some 20% of the chain is in the segmentally mobile form, regardless of ionic strength, and that its composition is highly hydrophobic, with few polar side chains. This suggests the possibility that this part of the molecule may penetrate into the lipid bilayer. Conformational stability of the spectrin dimer, as measured by circular dichroism, is substantially unaffected by the state of phosphorylation and by the ionic strength, even though the latter is known to affect the size or shape of the molecule.

Humans↗
PubMed1979

In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte.

The formation of a high-molecular weight complex between spectrin and F-actin depends on the presence of a third cytoskeletal constituent, protein 4.1. Electron microscopy shows that in this ternary complex the actin filaments are linked by bridges, which have the appearance of spectrin. The spectrin must be in the tetrameric state for such bridges to form: the dimer is evidently univalent, for it binds but forms no cross-links. G-actin also fails to form extended complexes. It is inferred that in the native cytoskeleton the spectrin is tetrameric and associated with 4.1 and probably oligomers of actin.

Actins↗
PubMed1977

An RNA core in the 30S ribosomal subunit of Escherichia coli and its structural and functional significance.

1. Evidence is presented for the occurrence of a very stable RNA core (S4-RNA) in "native" 16S RNA that is also present in the 30S subunit of Escherichia coli. A model giving the approximate location of this RNA core in the 30S subunit is presented. 2. It is proposed (a) that this S4-RNA acts as a nucleus for the assembly of the 30S subunit, and (b) that a small class of "linkage" proteins, including S4, further facilitate the assembly of the proteins to the RNA, thereby explaining some of the "cooperative" effects that are observed during in vitro assembly. 3. Evidence for the importance of the RNA core in the functioning of the ribosome is discussed.

Bacteria↗
PubMed1975

An investigation of the 16-S RNA binding sites of ribosomal proteins S4, S8, S15, and S20 FROM Escherichia coli.

The RNA binding sites of four 30-S ribosomal subunit proteins from Escherichia coli, namely S4, S8, S15, and S20 were prepared from reconstituted single protein - 16-S-RNA complexes by mild enzymic digestion of non-protected RNA regions. Oligonucleotide fingerprints of the protected RNA regions were obtained and their positions were located within the 16-S-RNA sequence. They were not completely contiguous regions of RNA; oligonucleotides had been excised from each of them. The binding sites of S4 and S20, and those of S8 and S15 showed overlapping. The specificity of the RNA binding sites was confirmed by a reconstitution method.

Bacterial Proteins↗
PubMed1975

Evidence for tertiary structural RNA-RNA interactions within the protein S4 binding site at the 5'-end of 16S ribosomal RNA of Escherichia coli.+.

Evidence is presented for tertiary structural interaction(s) (interactions(s) between two regions of an RNA molecule that are widely separated in the RNA sequence) within the 5'-one third of the 16S ribosomal RNA of Escherichia coli that constitutes the binding site of protein S4. The two main interacting RNA regions were separated by about 120 nucleotides (sections Q to M) of the 16S RNA sequence. A second, smaller gap, of 13 nucleotides, occurred within section C". The two main interacting regions contain about 150 nucleotides (sections H" to Q) and 160 nucleotides (sections M to C"). They are folded back on one another and, especially in the presence of protein S4, are strongly protected against ribonuclease digestion. The intermediate region (sections Q to M), however, is relatively accessible to ribonucleases in the S4-RNP. By partial removal of subfragments from the RNA complex it was possible to localise the two main interacting sites within sections H" - H and sections I" - C". Three main criteria for the specificity of the RNA-RNA interactions were invoked and satisfied. The possibility of other tertiary structural RNA-RNA interactions occurring in other regions of the 16S RNA is discussed. Finally, all the structural information on the S4-RNP is summarised and a tentative model is proposed.

Base Sequence↗
PubMed1975

Location and characteristics of ribosomal protein binding sites in the 16S RNA of Escherichia coli.

Specific binding sites for five proteins of the Escherichia coli 30S ribosomal subunit have been located within the 16S RNA. The sites are structurally diverse and range in size from 40 to 500 nucleotides; their functional integrity appears to depend upon both the secondary structure and conformation of the RNA molecule. Evidence is presented which indicates that additional proteins interact with the RNA at later stages of subunit assembly.

Bacterial Proteins↗