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Two distinct yolk lipoprotein complexes from Caenorhabditis elegans
W J Sharrock1, M E Sutherlin, K Leske
1Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul 55108.
The Journal of Biological Chemistry
|August 25, 1990
Summary
The nematode Caenorhabditis elegans yolk contains two distinct lipoprotein complexes. One complex includes yp170A, yp115, and yp88 proteins, while the other consists of yp170B proteins.
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- The nematode Caenorhabditis elegans utilizes yolk proteins for embryonic development.
- Yolk proteins are organized into lipoprotein particles of varying sizes (8S and 12S).
- The precise subunit composition of these lipoprotein complexes remains unclear.
Purpose of the Study:
- To elucidate the subunit composition of Caenorhabditis elegans yolk lipoproteins.
- To differentiate between the two identified lipoprotein complexes.
Main Methods:
- Immunoaffinity binding assays using specific polyclonal and monoclonal antibodies.
- Analysis of polypeptide interactions under non-denaturing conditions.
- Investigation of disulfide bond formation to infer protein associations.
Main Results:
- Two distinct yolk lipoprotein complexes were identified in C. elegans.
- The 'A complex' comprises yp170A, yp115, and yp88, forming a heterodimeric structure.
- The 'B dimer' consists of yp170B, which self-associates into dimers.
Conclusions:
- C. elegans yolk lipoproteins exist as two discrete complexes, A and B.
- Complex A is a heterodimer, while Complex B is a homodimer.
- These findings clarify the molecular organization of nematode yolk.