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PMID: 287002 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The lambda repressor contains two domains.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 4 ·1979-04-00 ·Pages 1608-12

Pabo CO, Sauer RT, Sturtevant JM, Ptashne M

Abstract

Papain digestion of the lambda phage repressor produces two fragments that are relatively resistant to further digestion. One includes the amino terminus (residues 1-92) and the other the carboxyl terminus (residues 132-236). Calorimetry shows that the amino-terminal fragment denatures near 50 degrees C and that the carboxyl-terminal fragment denatures near 70 degrees C. Intact repressor undergoes two denaturations, one near 50 degrees C and another near 70 degrees C. These and other data show that lambda repressor consists of two domains joined by a "connector" 40 amino acids long that is sensitive to proteases. The amino-terminal domain binds DNA, and the carboxyl-terminal domain oligomerizes.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Coliphages/analysis Molecular Weight Papain Peptide Fragments/analysis Protein Denaturation Repressor Proteins Transcription Factors
Chemicals
Amino Acids Peptide Fragments Repressor Proteins Transcription Factors Papain
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pabo C O
Sauer R T
Sturtevant J M
Ptashne M
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23 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.76.4.1608
Published
1979-04-00
Pages
1608-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383439
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.76.4.1608 PMC Full Text View journal details
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