alpha-factor secretion signal

N-terminal secretion signal from S. cerevisiae alpha-factor.
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250 200 150 100 50 End (267) BsrDI (215) PsiI (196) MmeI (191) AcuI (125) ApoI (95) HincII (66) BstAPI (55) BpmI (44) PstI (27) SfcI (23) Start (0) presequence pro region α- factor secretion signal 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).
AcuI  (125)
1 site
C T G A A G ( N ) 14 N N G A C T T C ( N ) 14

Cleavage may be enhanced when more than one copy of the AcuI recognition sequence is present.
Sticky ends from different AcuI sites may not be compatible.
After cleavage, AcuI can remain bound to DNA and alter its electrophoretic mobility.
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
3 segments
   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
3 segments
   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
3 segments
   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.
ORF:  1 .. 267  =  267 bp
ORF:  89 amino acids  =  9.4 kDa
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Download alpha-factor secretion signal.dna file

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