The myb oncogene product induces DNA-bending

Pothana Saikumar, Jerome L. Gabriel, E. Premkumar Reddy

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The nuclear oncogene v-myb and its cellular counterpart c-myb code for proteins that bind to DNA in a sequence specific manner and act as regulators of transcription. The Myb protein contains DNA binding and transregulatory domains which are important for its function. The DNA binding domain of Myb protein has been shown to contain three imperfectly conserved repeats of 50-52 aminoacids that constitute the amino terminal end. In this communication, we show that Myb protein induces conformational change in DNA after protein-DNA complex formation. Circular permutation assays indicate that Myb protein induces DNA bending at the site of binding. Phasing analysis confirm the DNA bending and allowed the detection of relative orientation of bend. Myb proteins which comprise only DNA-binding domains either with three repeats or two repeats also bend DNA in the same orientation as the larger proteins with both DNA-binding and transactivating domains. However, the transactivating region seems to influence the magnitude of bend angle. We used molecular modeling to analyse the structure of Myb-DNA complex formation resulting in the bending of DNA. Data presented here show that Myb protein, like other transcriptional regulators, bends DNA upon binding allowing the interaction of regulatory elements.

Original languageEnglish (US)
Pages (from-to)1279-1287
Number of pages9
JournalOncogene
Volume9
Issue number4
StatePublished - Apr 1994

Fingerprint

myb Genes
Oncogene Proteins
DNA
Proteins
Proto-Oncogene Proteins c-myb
DNA-Binding Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

Cite this

Saikumar, P., Gabriel, J. L., & Reddy, E. P. (1994). The myb oncogene product induces DNA-bending. Oncogene, 9(4), 1279-1287.

The myb oncogene product induces DNA-bending. / Saikumar, Pothana; Gabriel, Jerome L.; Reddy, E. Premkumar.

In: Oncogene, Vol. 9, No. 4, 04.1994, p. 1279-1287.

Research output: Contribution to journalArticle

Saikumar, P, Gabriel, JL & Reddy, EP 1994, 'The myb oncogene product induces DNA-bending', Oncogene, vol. 9, no. 4, pp. 1279-1287.
Saikumar P, Gabriel JL, Reddy EP. The myb oncogene product induces DNA-bending. Oncogene. 1994 Apr;9(4):1279-1287.
Saikumar, Pothana ; Gabriel, Jerome L. ; Reddy, E. Premkumar. / The myb oncogene product induces DNA-bending. In: Oncogene. 1994 ; Vol. 9, No. 4. pp. 1279-1287.
@article{7ca4c97f628f46cdae46791ef4bf8898,
title = "The myb oncogene product induces DNA-bending",
abstract = "The nuclear oncogene v-myb and its cellular counterpart c-myb code for proteins that bind to DNA in a sequence specific manner and act as regulators of transcription. The Myb protein contains DNA binding and transregulatory domains which are important for its function. The DNA binding domain of Myb protein has been shown to contain three imperfectly conserved repeats of 50-52 aminoacids that constitute the amino terminal end. In this communication, we show that Myb protein induces conformational change in DNA after protein-DNA complex formation. Circular permutation assays indicate that Myb protein induces DNA bending at the site of binding. Phasing analysis confirm the DNA bending and allowed the detection of relative orientation of bend. Myb proteins which comprise only DNA-binding domains either with three repeats or two repeats also bend DNA in the same orientation as the larger proteins with both DNA-binding and transactivating domains. However, the transactivating region seems to influence the magnitude of bend angle. We used molecular modeling to analyse the structure of Myb-DNA complex formation resulting in the bending of DNA. Data presented here show that Myb protein, like other transcriptional regulators, bends DNA upon binding allowing the interaction of regulatory elements.",
author = "Pothana Saikumar and Gabriel, {Jerome L.} and Reddy, {E. Premkumar}",
year = "1994",
month = "4",
language = "English (US)",
volume = "9",
pages = "1279--1287",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "4",

}

TY - JOUR

T1 - The myb oncogene product induces DNA-bending

AU - Saikumar, Pothana

AU - Gabriel, Jerome L.

AU - Reddy, E. Premkumar

PY - 1994/4

Y1 - 1994/4

N2 - The nuclear oncogene v-myb and its cellular counterpart c-myb code for proteins that bind to DNA in a sequence specific manner and act as regulators of transcription. The Myb protein contains DNA binding and transregulatory domains which are important for its function. The DNA binding domain of Myb protein has been shown to contain three imperfectly conserved repeats of 50-52 aminoacids that constitute the amino terminal end. In this communication, we show that Myb protein induces conformational change in DNA after protein-DNA complex formation. Circular permutation assays indicate that Myb protein induces DNA bending at the site of binding. Phasing analysis confirm the DNA bending and allowed the detection of relative orientation of bend. Myb proteins which comprise only DNA-binding domains either with three repeats or two repeats also bend DNA in the same orientation as the larger proteins with both DNA-binding and transactivating domains. However, the transactivating region seems to influence the magnitude of bend angle. We used molecular modeling to analyse the structure of Myb-DNA complex formation resulting in the bending of DNA. Data presented here show that Myb protein, like other transcriptional regulators, bends DNA upon binding allowing the interaction of regulatory elements.

AB - The nuclear oncogene v-myb and its cellular counterpart c-myb code for proteins that bind to DNA in a sequence specific manner and act as regulators of transcription. The Myb protein contains DNA binding and transregulatory domains which are important for its function. The DNA binding domain of Myb protein has been shown to contain three imperfectly conserved repeats of 50-52 aminoacids that constitute the amino terminal end. In this communication, we show that Myb protein induces conformational change in DNA after protein-DNA complex formation. Circular permutation assays indicate that Myb protein induces DNA bending at the site of binding. Phasing analysis confirm the DNA bending and allowed the detection of relative orientation of bend. Myb proteins which comprise only DNA-binding domains either with three repeats or two repeats also bend DNA in the same orientation as the larger proteins with both DNA-binding and transactivating domains. However, the transactivating region seems to influence the magnitude of bend angle. We used molecular modeling to analyse the structure of Myb-DNA complex formation resulting in the bending of DNA. Data presented here show that Myb protein, like other transcriptional regulators, bends DNA upon binding allowing the interaction of regulatory elements.

UR - http://www.scopus.com/inward/record.url?scp=0028174134&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028174134&partnerID=8YFLogxK

M3 - Article

C2 - 8134132

AN - SCOPUS:0028174134

VL - 9

SP - 1279

EP - 1287

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 4

ER -