486 A. TSUGITA AND II. FRAENKEL-CONRAT 



longest one by the two research groujjs, and the few differences remaining 

 between our sequences (Tsujrita et al., 1960, 1962a) and the recently 

 corrected ones of Andcrcr (1962) will probably be soon resolved. 



Tn order to obtain the sequential arrangement of the peptides, Witt- 

 niann (1960a) investigated the tiypsin split products of several natural 

 mutants characterized by fewer arginine and/or lysine residues than the 

 common strain. From the comjiarison between the number and composi- 

 tion of the peptides obtained from the wild tyj^e and those from such 

 mutants the order of some of the jx'ptides has tentatively been estab- 

 lisluMl. The results were confirmed and extended bv studies of the basic 



Acetyl N-Scf^Tyr— ••Ser-»'lleu- 



„„,.-.„„ .) 



V Leu-^Gly — ►Asp— ►Glu— ►Phe— ►Glu — ►Ihr — ►ijiu — ►Ciiu — ►Ala— •<Arg)— ►! nr— ►vol — ►(jiu — ►«! ->^ 



Cvai'« — I nr'W — VQi^ UIU'^ — rro'* — oef^— rru'^ — Lyb^— i ry^ — vui^ — oiu'^ — aef^ — nnf^ — oiu'^— tMrq) m 

 (Arq)-frPhe-^Pro — ►Asp-^Sef — ►Asp-^Phe— •{Us)— ►Vol — ►Tyr— •{Q)— ►Tyr— ►Asp— ►Ala— ►Vol ■>^ 



90 85 80 } 



C(ArQ)«— Thr-«— Asp-*— Phe-«-Ala-« — Gly«— Leu-4— Leu-*— Alo-* — Thr*— Vol-*— Leu-«— Pro*— Asp-*— LeiJ« 

 NHp - 95 NH2 NH2 NH2 100 NH2 105 



Asp-^(Argi)-^lleu — ►lieu— ►Glu — ►Vol— ►Glu — ►Asp-^GIu — ►•Alo— ►Asp-^Pro— ►Thr— ►Thr— ».AIa -^^ 



120 H5 . ~ no . J 



(Alo*— Vol-* — Thr-* — Ala-*— Asp-*— Asp-*-Val-* — Arg-*— (Arq)* — ^Thr-*— Ala*— Asp-*-Leu^— Thr-*— Glu M 

 125 NH^ 130 ^-^ 135 



lieu— ♦^rgi-*Ser — ►Ala— ►Asp— ►lieu — ►-■asD-^/eo — ►*»l/— ►vo/— ►cs/u— »-Leu— ►lieu — •(Arg)— ►Gly ^ 



150 145 ,^ 140 NH2 J 



CI pii*-rj«-* — Crff-* — ^er-*-Ser-* — Glu*— Phe-* — Ser-* — Ser-*— (Ara>*— Asp-*— Tvr* — Ser-* — Gly* — Thr 4i 



Vol— ►Try— ►Thr — ► Ser -►Gly— ► Pro-frAio 



Fig. 3. Amino acid scqiieiK-e of protein from common TMV. This sequence is 

 based on all information available in February 1962. It now appears (June 1962) 

 that one inversion (residues 25, 26) is necessary to correct the structure previously 

 published from our laboratory (Tsugita et al., 1960; Tsugita et al., 1962a). About 

 five changes have been made in the structure reported by Anderer ct al. (1960b; 

 Anderer, 1962). All but the positions of a few amide groups appear to be agreed 

 upon. 



peptides obtained by chymotrypsin and subtilisin which supplied the 

 overlapping sequences needed to align all tryptic peptides in a unique 

 order (Anderer et al, 1960b; Tsugita et al, 1960). By these efforts the 

 amino acid sequence of the TMV-protein has been determined almost 

 completely in each of the two laboratories, and since the minor uncer- 

 tainties do not overlap, the entire sequence can be regarded as known 



