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Table 1 Insect beta tubulin sequence features.

From: Tubulin evolution in insects: gene duplication and subfunctionalization provide specialized isoforms in a functionally constrained gene family

Isoform

Function

Average and maximum pairwise distances

-COOH terminus sequence

Post-translational modification sites/Conserved sequence features

  

Drosophila

Mosquito

All Insects

  

β1

Major isoform

0.000 +/- 0.000

(n = 12)

0.002 +/- 0.002

(n = 2)

Average

0.011 +/- 0.003

(n = 9)

Maximum 0.027

(n = 10)

Ha β1a EATADDEAE FEEEGEVEGE YA

Ha β1b EATADDEAE FEEEGEVEGE YD

Dm β1 EATADEDAE FEEEQEAEVD EN

Ae β1 EATADEDAE FDEEQEAEVD EN

Ag β1 EATADEDAE FDEEQEAEVD EN

Bm β1a EATADEDAE FDEEQEQEIE DN

Bm β1b EATADEDAE FDEEQEQEIE EH

Tc β1 EATADEDAE FDEEQEAEVD EN

Nv β1a -

Nv β1b TMNGPRDAP DEDVEVVEEE LRD

Am β1 EATADEDAE FDEEQEAEVD EN

Ap β1 EATADEEAE FDEEQEQEVD EN

Ph β1 EATADEDAE FDEEQEEVVD EN

PTM sites

Polyglutamylation - yes

Polyglycylation - yes

Phosphorylation - yes

β2

Testis-specific isoform

0.000 +/- 0.000

(n = 12)

0.060 +/- 0.011

(n = 2)

Average

0.085 +/- 0.009

(n = 9)

Maximum 0.464

(n = 17)

Dm β2 EATADEEGE FDEDEEGGGD E

Ae β2 EATADEEGE FDEEEEGGEE

Ag β2 EATADDEGE MDEEEEGGED

Bm β2 DATADDEGE FDEEAEEGLE E

Tcβ2a DATAEEEGE FDEEEEGDNE GEN

Tc β2b DAEVDEEYG DEDETEEDKF EEET

Nv β2a EATAEEDTE FDEDEGENEG N

Nv β2b EATADEFAD YEEDEEEEED YA

Nv β2c EATTEE--D FETEDAGDD FETCDQE

Am β2a EATAEEEGE FDEEEEGEGE HP

Am β2b EATAEDEGE FDEEEETEK

Apβ2a DATVDEDGE GDDDEEDADA

Apβ2b EATIDETGE-EDEDEDADA

Apβ2c DATVDEEGE GDDDDEDAEA

Apβ2d EATVDAPGG VNEE

Ph β2a EATADEEGE DEEDEGGED

Ph β2b EATSYEYDE DEGEENEVEE EEEKEMTNWL PA

PTM sites

Polyglutamylation - yes, except Apβ2d

Polyglycylation -- yes, except Apβ2d

Phosphorylation -- yes

Conserved sequence features

Axoneme motif - yes, except Agβ2, Tcβ2b, Nvβ2a-c,

Apβ2a-d, Phβ2a, b

Gly56-- yes, except Phβ2b

β3

Minor isoform expressed in variety of pre-adult mesodermal and neural domains

0.009 +/- 0.002

(n = 10)

0.014 +/- 0.005

(n = 2)

Average 0.092 +/- 0.010

(n = 9)

Maximum 0.148

(n = 9)

Dm β3 EATADDEFD PEVNQEEVEG DCI

Ae β3 EATADDEFE QEECADEMEG ECV

Ag β3 EATADDEFE QEDCQDEMEG ECV

Bm β3 EATAEDDTE FDQEDLEELA QDEHHD

Tc β3 EATADEEYE AEEEAAADDF NC

Nv β3 EATTEEDFE TEDAGDDFET CDQE

Am β3 EATAEEDFE AEECADDFET CDQE

Ap β3 EASVDEEYI EEEETEETDM CD

Ph β3 LYISTIIKI

PTM sites

Polyglutamylation -- yes

Polyglycylation -- yes, except Tcβ3, Nvβ3, Amβ3, Nvβ3, Apβ3

Phosphorylation - yes

Conserved sequence features

Nucleotide-binding domain amino acid insert (aa56) - yes

β4

Minor isoform, pre-adult tissues in Dm , absent in Bm)

0.032 +/- 0.005

(n = 11)

0.104 +/- 0.012

(n = 3)

Average 0.136 +/- 0.015

(n = 5)

Maximum 0.186

(n = 6)

Dm β4 EATADDEVE FDDEQAEQEG YESEVLQNGN GE

Ae β4a EASADDYVE GEHDFDDEEE IQQ

Ae β4b DASVEDYED GEEMIEEEGE QHVE

Ag β4 DAEVEDYDE MEEIPEEEQQ QQQE

Ap β4 EATAEEVEF DDEEVVEEVD DNKDY

Ph β4 VRSSLHLSN AANIEIQKNE ILNRNT

PTM sites

Polyglutamylation - ? Polyglycylation - ?

Phosphorylation - yes

  1. Features of the four beta tubulin isoforms identified in insects are presented. The function and/or expression domain of each sequence in D. melanogaster [16, 17] and B. mori [35], the two insects in which tubulin expression and function have been studied, are presented in Column 2. Average and maximum pairwise distance calculations in Column 3 refer to the average # amino acid differences/site among conserved isoforms, and the maximum pairwise distance between any two orthologs, including divergent duplication products, respectively. For "all insects", the only Drosophila species included is Dm, to avoid a Dipteran skew in the results. CTT sequences are presented in Column 4, for purposes of inspection as they constitute ~50% of the differences among tubulins. Tubulin post-translational modifications (PTMs) occur on sequence motifs whose presence and absence are presented in the Column 5. Polyglutamylation and polyglycylation sequence motifs are degenerate, the "?" indicates that a potentially modifiable, but experimentally uncharacterized residue(s) is present for these PTMs. Unusual sequence features or motifs known to mediate specific tubulin functional specializations are also noted. The full-length sequences for Nvβ1, Phβ3, Dpβ3, Dsβ3 were not available. Key: Pediculus humanus corporisPh, Acyrthosiphon pisum Ap, Apis millifera Am, Nasonia vitripennis Nv, Tribolium castenatum Tc, Bombyx mori Bm, Aedes aegypti Ae, Anopheles gambiae Ag, Drosophila melanogaster Dm, D. sechellia Dc, D. yakuba Dy, D. erecta De, D. simulans Ds, D. mojavensis Do, D. grimshawi Dg, D. ananassae Da, D. persimilis Dp, D. psuedoobscura Du, D. virilis Dv, D. willistoni Dw).