scholarly journals Phage lambda Cro protein and cI repressor use two different patterns of specific protein-DNA interactions to achieve sequence specificity in vivo.

Genetics ◽  
1989 ◽  
Vol 121 (1) ◽  
pp. 5-12
Author(s):  
N Benson ◽  
P Youderian
Keyword(s):  
Specific Protein ◽  
Specific Interactions ◽  
Sequence Specificity ◽  
Base Pairs ◽  
Lambda Repressor ◽  
Protein Dna Interactions ◽  
Cro Protein ◽  
Data Call ◽  
Half Site

Abstract By assaying the binding of wild-type Cro to a set of 40 mutant lambda operators in vivo, we have determined that the 14 outermost base pairs of the 17 base pair, consensus lambda operator are critical for Cro binding. Cro protein recognizes 4 base pairs in a lambda operator half-site in different ways than cI repressor. The sequence determinants of Cro binding at these critical positions in vivo are nearly perfectly consistent with the model proposed by W. F. ANDERSON, D. H. OHLENDORF, Y. TAKEDA and B. W. MATTHEWS and modified by Y. TAKEDA, A. SARAI and V. M. RIVERA for the specific interactions between Cro and its operator, and explain the relative order of affinities of the six natural lambda operators for Cro. Our data call into question the idea that lambda repressor and Cro protein recognize the consensus lambda operator by nearly identical patterns of specific interactions.

DNA bending by Cro protein in specific and nonspecific complexes: implications for protein site recognition and specificity

Science ◽  
1994 ◽  
Vol 266 (5190) ◽  
pp. 1562-1566 ◽  
Author(s):  
D. Erie ◽  
G Yang ◽  
H. Schultz ◽  
C Bustamante
Keyword(s):  
Dna Bending ◽  
Cro Protein ◽  
Site Recognition

scholarly journals Mechanism of action of the cro protein of bacteriophage lambda.

1978 ◽  
Vol 75 (4) ◽  
pp. 1783-1787 ◽  
Author(s):  
A. Johnson ◽  
B. J. Meyer ◽  
M. Ptashne
Keyword(s):  
Mechanism Of Action ◽  
Bacteriophage Lambda ◽  
Cro Protein

scholarly journals Thermodynamics of Cro protein-DNA interactions.

1992 ◽  
Vol 89 (17) ◽  
pp. 8180-8184 ◽  
Author(s):  
Y. Takeda ◽  
P. D. Ross ◽  
C. P. Mudd
Keyword(s):  
Dna Interactions ◽  
Protein Dna Interactions ◽  
Cro Protein

Studies on the crystallization of the cro protein-pseudo OR3 complex

1986 ◽  
Vol 76 (3) ◽  
pp. 715-718
Author(s):  
Richard G. Brennan ◽  
Jim Kim ◽  
Yoshinori Takeda ◽  
Wayne F. Anderson ◽  
Brian W. Matthews
Keyword(s):  
Cro Protein

Folding Kinetics of Phage 434 Cro Protein†

Biochemistry ◽  
2000 ◽  
Vol 39 (45) ◽  
pp. 13963-13973 ◽  
Author(s):  
D. V. Laurents ◽  
S. Corrales ◽  
M. Elías-Arnanz ◽  
P. Sevilla ◽  
M. Rico ◽  
...  
Keyword(s):  
Folding Kinetics ◽  
Cro Protein ◽  
Kinetics Of

scholarly journals Identification of the Repressor-Encoding Gene of the Lactobacillus Bacteriophage A2

1998 ◽  
Vol 180 (13) ◽  
pp. 3474-3476 ◽  
Author(s):  
Victor Ladero ◽  
Pilar García ◽  
Victoria Bascarán ◽  
Mónica Herrero ◽  
Miguel A. Alvarez ◽  
...  
Keyword(s):  
Dna Binding ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Repressor Gene ◽  
Encoding Gene ◽  
Cro Protein ◽  
Residue Polypeptide

ABSTRACT The repressor gene of the Lactobacillus phage A2 has the following properties: it (i) encodes a 224-residue polypeptide with DNA binding and RecA cleavage motifs, (ii) is expressed in lysogenic cultures, and (iii) confers superinfection immunity on the host. Adjacent, but divergently transcribed, lies another open reading frame whose product resembles the λ Cro protein. In the 161-bp intergenic segment, putative promoters and operators have been detected.

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