A multifunctional protein: involvement of the alpha-1 serum protease inhibitor in SDS and high salt-stable DNA-protein complexes.
Occasionally new and intriguing roles arise for proteins with well established functions. The alpha-1 serum protease inhibitor (alpha-1 PI) represents another example. Sequence identities exist in the alpha-1 PI and in a nuclear 52-kDa glycoprotein which is involved in resistant DNA-polypeptide complexes. The results of Western blots support the identity of the two proteins and immunocytochemical studies indicate the nuclear location of the alpha-1 PI. Consistently, e.g. Ehrlich ascites tumor cells express the alpha-1 PI, and the fusion protein between the alpha-1 PI and the green fluorescent protein from Aequorea victoria shows intracellular accumulation and partly nuclear location.
Glaser
T
T
Division Biochemistry of the Cell (0225), German Cancer Research Center, Heidelberg.
Rothbarth
K
K
Stammer
H
H
Kempf
T
T
Spiess
E
E
Werner
D
D
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002286:Carcinoma, Ehrlich Tumor / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D019286:Endopeptidase K / Q000494:pharmacology; D019084:Fluorescent Antibody Technique, Indirect; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D000515:alpha 1-Antitrypsin / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure
D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D000515:alpha 1-Antitrypsin; D012967:Sodium Dodecyl Sulfate; D019286:Endopeptidase K