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Plasmid Files

α-factor secretion signal

N-terminal secretion signal from S. cerevisiae alpha-factor.

 
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 250 200 150 100 50 presequence pro region α- factor secretion signal End (267) BsrDI (215) PsiI (196) MmeI (191) ApoI (95) HincII (66) BstAPI (55) BpmI (44) PstI (27) SfcI (23) Start (0) α- factor secretion signal 267 bp
End  (267)
0 sites
BsrDI  (215)
1 site
G C A A T G N N C G T T A C

Sticky ends from different BsrDI sites may not be compatible.
PsiI  (196)
1 site
T T A T A A A A T A T T
MmeI  (191)
1 site
T C C R A C ( N ) 18 N N A G G Y T G ( N ) 18

Efficient cleavage requires at least two copies of the MmeI
recognition sequence.
Sticky ends from different MmeI sites may not be compatible.
For full activity, add fresh S-adenosylmethionine (SAM).
ApoI  (95)
1 site
R A A T T Y Y T T A A R

ApoI is typically used at 50°C, but is 50% active at 37°C.
HincII  (66)
1 site
G T Y R A C C A R Y T G
BstAPI  (55)
1 site
G C A N N N N N T G C C G T N N N N N A C G

Sticky ends from different BstAPI sites may not be compatible.
BpmI  (44)
1 site
C T G G A G ( N ) 14 N N G A C C T C ( N ) 14

Efficient cleavage requires at least two copies of the BpmI
recognition sequence.
Sticky ends from different BpmI sites may not be compatible.
After cleavage, BpmI can remain bound to DNA and alter its
electrophoretic mobility.
BpmI quickly loses activity at 37°C.
PstI  (27)
1 site
C T G C A G G A C G T C
SfcI  (23)
1 site
C T R Y A G G A Y R T C

Sticky ends from different SfcI sites may not be compatible.
SfcI quickly loses activity at 37°C, but can be used at 25°C for long
incubations.
Start  (0)
0 sites
α-factor secretion signal
1 .. 267  =  267 bp
89 amino acids  =  9.4 kDa
   Segment 1:  presequence  
   1 .. 57  =  57 bp
   19 amino acids  =  2.0 kDa
Product: N-terminal secretion signal from S.
cerevisiae
alpha-factor
Cleavage by the Kex2 protease occurs after the
dibasic KR sequence. The EA dipeptides are then
removed by dipeptidyl aminopeptidase A.
α-factor secretion signal
1 .. 267  =  267 bp
89 amino acids  =  9.4 kDa
   Segment 2:  pro region  
   58 .. 255  =  198 bp
   66 amino acids  =  7.0 kDa
Product: N-terminal secretion signal from S.
cerevisiae
alpha-factor
Cleavage by the Kex2 protease occurs after the
dibasic KR sequence. The EA dipeptides are then
removed by dipeptidyl aminopeptidase A.
α-factor secretion signal
1 .. 267  =  267 bp
89 amino acids  =  9.4 kDa
   Segment 3:  
   256 .. 267  =  12 bp
   4 amino acids  =  418.4 Da
Product: N-terminal secretion signal from S.
cerevisiae
alpha-factor
Cleavage by the Kex2 protease occurs after the
dibasic KR sequence. The EA dipeptides are then
removed by dipeptidyl aminopeptidase A.
α-factor secretion signal
1 .. 267  =  267 bp
89 amino acids  =  9.4 kDa
3 segments
Product: N-terminal secretion signal from S.
cerevisiae
alpha-factor
Cleavage by the Kex2 protease occurs after the
dibasic KR sequence. The EA dipeptides are then
removed by dipeptidyl aminopeptidase A.
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