Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1994-10-31
|
| pubmed:abstractText |
The reported cDNA structure of chicken smooth muscle myosin light chain kinase (smMLCK) encodes a protein of 972 residues (Olson et al. Proc. Natl. Acad. Sci USA, 87:2284-2288, 1990). The calculated M(r) is 107,534 whereas the estimate by SDS-PAGE is approximately 130,000. Gibson and Higgins (DNA Sequence (in press)) have recently reported the possibility of errors in the cDNA sequence for non-muscle MLCK and that the NH2-terminus of both it and smMLCK may extend beyond the reported coding region. The native smMLCK is NH2-terminally blocked. A CNBr peptide derived from smMLCK contains the NH2-terminal sequence Asp-Phe-Arg-Ala corresponding to residues 2 to 4 in the smMLCK sequence indicating that Met-1 is present. Using a limited thermolysin digest we isolated an NH2-terminally blocked peptide by reversed-phase HPLC. This thermolytic peptide had a mass of approximately 797 by time of flight mass spectrometry. Amino acid analysis and Edman sequencing of a CNBr-subfragment of the thermolytic peptide indicated that it had the composition and sequence, (Met)-Asp-Phe-Arg-Ala-Asn, with a calculated mass of 753. The difference in mass corresponds to the NH2-terminal Met being blocked by acetylation. The results demonstrate that the NH2-terminal sequence of smMLCK inferred from the reported cDNA sequence is correct and that the proposed initiating Met is not removed, but modified by alpha-NH2 acetylation of the translation product.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0300-8177
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
127-128
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
81-91
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:7935365-Acetylation,
pubmed-meshheading:7935365-Amino Acid Sequence,
pubmed-meshheading:7935365-Animals,
pubmed-meshheading:7935365-Base Sequence,
pubmed-meshheading:7935365-Chickens,
pubmed-meshheading:7935365-Chromatography, High Pressure Liquid,
pubmed-meshheading:7935365-Consensus Sequence,
pubmed-meshheading:7935365-Cyanogen Bromide,
pubmed-meshheading:7935365-DNA, Complementary,
pubmed-meshheading:7935365-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7935365-Endopeptidases,
pubmed-meshheading:7935365-Gizzard,
pubmed-meshheading:7935365-Mass Spectrometry,
pubmed-meshheading:7935365-Methionine,
pubmed-meshheading:7935365-Molecular Sequence Data,
pubmed-meshheading:7935365-Muscle, Smooth,
pubmed-meshheading:7935365-Myosin-Light-Chain Kinase,
pubmed-meshheading:7935365-Peptide Fragments
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Chicken smooth muscle myosin light chain kinase is acetylated on its NH2-terminal methionine.
|
| pubmed:affiliation |
St. Vincent's Institute of Medical Research, Fitzroy Vic., Australia.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|