Abstract
Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 71-80 |
| Number of pages | 10 |
| Journal | Genes and Development |
| Volume | 6 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1992 |
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All Science Journal Classification (ASJC) codes
- Genetics
- Developmental Biology
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Myc and Max associate in vivo. / Blackwood, E. M.; Luscher, B.; Eisenman, R. N.
In: Genes and Development, Vol. 6, No. 1, 01.01.1992, p. 71-80.Research output: Contribution to journal › Article
TY - JOUR
T1 - Myc and Max associate in vivo
AU - Blackwood, E. M.
AU - Luscher, B.
AU - Eisenman, R. N.
PY - 1992/1/1
Y1 - 1992/1/1
N2 - Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes.
AB - Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes.
UR - http://www.scopus.com/inward/record.url?scp=0026576604&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026576604&partnerID=8YFLogxK
U2 - 10.1101/gad.6.1.71
DO - 10.1101/gad.6.1.71
M3 - Article
C2 - 1730411
AN - SCOPUS:0026576604
VL - 6
SP - 71
EP - 80
JO - Genes and Development
JF - Genes and Development
SN - 0890-9369
IS - 1
ER -